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2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinone + ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-decylbenzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-decylbenzoquinone + 2 ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + ferrocytochrome c + H+ [side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethyl-7,11,15,19,23,27,31,35,39-hentetracontanonaen-1-yl]-5,6-dimethoxy-3-methyl-1,4-benzenediol + 2 ferricytochrome c
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethylhentetraconta-7,11,15,19,23,27,31,35,39-nonaen-1-yl]-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione + 2 ferrocytochrome c + 2 H+
-
ubiquinone-like compound with a hydroxyl-substituted side chain exhibits substrate efficiencies below that of native ubiquinone but significantly higher efficiency than alpha-tocopheryl quinone
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
alpha-tocopheryl hydroquinone + ferricytochrome c + H+
alpha-tocopherol + ferrocytochrome c + H2O
-
-
-
-
?
coenzyme Q1H2 + 2 ferricytochrome c
coenzyme Q1 + 2 ferrocytochrome c + 2 H+
cytochrome b561 + ?
?
-
cytochrome b561, reduced upon flash excitation, is re-oxidized slowly even in the absence of antimycin
-
-
?
cytochrome c551 + ?
?
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
decylplastoquinol + 2 ferricytochrome c
decylplastoquinone + 2 ferrocytochrome c + 2 H+
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
dihydroubiquinone + ferricytochrome c
ubiquinone + ferrocytochrome c + 2 H+
-
-
-
?
menaquinol + 2 ferricytochrome c
menaquinone + 2 ferrocytochrome c + 2 H+
naphthoquinol + 2 ferricytochrome c
naphthoquinone + 2 ferrocytochrome c + 2 H+
-
-
naphthoquinone is the pool quinone of the organism
-
?
nonylubiquinol + 2 ferricytochrome c
nonylubiquinone + 2 ferrocytochrome c + 2 H+
plastohydroquinol + 2 ferricytochrome c
plastohydroquinone + 2 ferrocytochrome c + 2 H+
plastoquinol-1 + 2 ferricytochrome c
plastoquinone-1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastoquinol-9 + 2 ferricytochrome c
plastoquinone-9 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
quinol + 2 horse heart ferricytochrome c1
quinone + 2 horse heart ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
rhodoquinol-3 + 2 ferricytochrome c
rhodoquinone-3 + 2 ferrocytochrome c + 2 H+
-
a substrate-induced wQ-cycle bypass reaction leading to production of superoxide
i.e. 2-amino-5-farnesyl-3-methoxy-6-methyl-1,4-benzoquinone
-
?
tetramethyl-p-benzoquinol + cytochrome c
tetramethyl-p-benzoquinone + reduced cytochrome c
-
duroquinol
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
ubihydroquinol + cytochrome c
ubihydroquinone + reduced cytochrome c
ubiquinol + 2 4-carboxy-2,6-dinitrophenyllysine27-ferricytochrome c
ubiquinone + 2 4-carboxy-2,6-dinitrophenyllysine27-ferrocytochrome c + 2 H+
-
cytochrome c from horse, modified at Lys27
-
-
?
ubiquinol + 2 ferricyanide
ubiquinone + 2 ferrocyanide + 2 H+
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
ubiquinol + 2 ferricytochrome c2
ubiquinone + 2 ferrocytochrome c2 + 2 H+[side 2]
-
-
-
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
ubiquinol + ferricytochrome b-562
ubiquinone + ferrocytochrome b-562
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
ubiquinol + horse heart cytochrome c
?
ubiquinol + plastocyanin
?
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
ubiquinol 3 + cytochrome c
ubiquinone 3 + reduced cytochrome c
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
additional information
?
-
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
coenzyme Q1H2 + 2 ferricytochrome c
coenzyme Q1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
coenzyme Q1H2 + 2 ferricytochrome c
coenzyme Q1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
-
-
-
r
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylplastoquinol + 2 ferricytochrome c
decylplastoquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decylplastoquinol + 2 ferricytochrome c
decylplastoquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
-
horse heart cytochrome c, half of the center N sites was insensitive to decylubiquinol
-
-
?
menaquinol + 2 ferricytochrome c
menaquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
menaquinol + 2 ferricytochrome c
menaquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
nonylubiquinol + 2 ferricytochrome c
nonylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
nonylubiquinol + 2 ferricytochrome c
nonylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastohydroquinol + 2 ferricytochrome c
plastohydroquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastohydroquinol + 2 ferricytochrome c
plastohydroquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
-
-
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
-
-
-
-
?
ubihydroquinol + cytochrome c
ubihydroquinone + reduced cytochrome c
-
-
-
-
?
ubihydroquinol + cytochrome c
ubihydroquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + 2 ferricyanide
ubiquinone + 2 ferrocyanide + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricyanide
ubiquinone + 2 ferrocyanide + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
395300, 396001, 439942, 439943, 439944, 439945, 439946, 439947, 439948, 439949, 439950, 439952, 439953, 439955, 439956, 439958, 439960, 439961, 439962, 439964, 439966, 439967, 439970, 439975, 439978, 439979, 439980, 439983, 439985, 439986, 439988, 439989, 439990, 439991, 439993, 439995, 440000, 440003, 440005, 440006, 440009, 440012, 440016, 440018, 440020, 440023, 440025, 440026, 440027, 440028, 440029, 440030, 440035, 685360, 686076, 725396 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
395300, 439946, 439963, 439965, 439971, 439976, 439977, 439979, 439981, 439988, 439995, 440000, 440009, 440010, 440012, 440015, 440016, 440019, 440030, 440032, 440033, 440036, 724433, 724452, 725396, 725875 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
Fuscovulum blasticum
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
395300, 396001, 439942, 439945, 439946, 439951, 439954, 439955, 439962, 439967, 439969, 439972, 439977, 439987, 439988, 439990, 439992, 439994, 439997, 440000, 440004, 440015, 440017, 440024, 440030 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
396001, 439946, 439995, 440001, 440003, 440012, 440014, 440015, 440019, 685360, 724452 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
439946, 439976, 439998, 439999, 440003, 440010, 440012, 440015, 440019, 440021, 440022, 440030, 440036, 689387, 724452 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
under physiological conditions, the dimeric cytochrome bc1 complex is suggested to be continually primed by prompt oxidation of membrane ubiquinol via center N yielding a bound semiquinone in this center and a reduced, high-potential heme b in the other monomer of the enzyme. Then the oxidation of each ubiquinol molecule in center P is followed by ubiquinol formation in center N, proton translocation and generation of membrane voltage
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
395300, 439942, 439943, 439945, 439948, 439949, 439950, 439963, 439966, 439972, 439973, 439974, 439984, 439988, 439990, 439992, 439997, 440002, 440005, 440006, 440008, 440009, 440011, 440014, 440015, 440017, 440018, 440021, 440023, 440026, 440030, 440031, 685360, 724452 -
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
algal cytochrome c
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
-
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
-
-
-
-
?
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
-
-
-
-
?
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
binding interaction of ubiquinone with cytochrome b, overview
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
rate-limiting is the transfer of the first electron from ubiquinol to the [2Fe-2S] cluster of the Rieske iron-sulfur-protein at the Qo-side, reaction energy profile
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
r
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
activity is highest near physiological ionic strength and decreases at higher concentrations
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
substrate of chain length C5 to C10, ubiquinol binds transiently at the Qo site, only when both heme bL and the iron sulfur cluster are in the oxidized form, where it is oxidized
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
dihydroubiquinone-1 is not a suitable substrate, as it reacts nonenzymically with cytochrome c at a rapid rate
-
-
?
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
?
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
?
additional information
?
-
-
the cyt bc1 complex uses ubiquinol, but not plastoquinol, as a substrate, usage of a biomimetic oxidant, excited-state Ru(2,2'-dipyridyl)2(2-(2-pyridyl)benzimidazolate)+ in an aprotic medium to probe the oxidation of the ubiquinol analogue, 2,3-dimethoxy-5-methyl-1,4-benzoquinol, i.e. UQH2-0, and the plastoquinol analogue, trimethyl-1,4-benzoquinol, i.e. TMQH2-0, using time-resolved and steady-state spectroscopic techniques, comparison of isotope-dependent activation properties in the native and synthetic systems as well as analysis of the time-resolved direct-detection electron paramagnetic resonance signals in the synthetic system, overview
-
-
?
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
?
additional information
?
-
-
the Qo-cycle, overview
-
-
?
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
?
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
?
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
?
additional information
?
-
-
protonation reactions coupled to quinone binding, binding of 2.3-2.6 quinones per enzyme monomer at the Qo side, conformational changes
-
-
?
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
?
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
?
additional information
?
-
-
electron transfer takes place between the 2 cytochrome b subunits
-
-
?
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
?
additional information
?
-
-
model of half-of-the-sites activity in the dimeric cytochrome bc1 complex, overview
-
-
?
additional information
?
-
-
substrate synthesis and substrate specificity, overview
-
-
?
additional information
?
-
-
almost inert towards mammalian cytochrome c
-
-
?
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naphthoquinol + 2 ferricytochrome c
naphthoquinone + 2 ferrocytochrome c + 2 H+
-
-
naphthoquinone is the pool quinone of the organism
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
additional information
?
-
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
?
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
?
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
?
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
?
additional information
?
-
-
the Qo-cycle, overview
-
-
?
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
?
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
?
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
?
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
?
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
?
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
?
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2,3,4-trimethoxy-5-decyl-6-methyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibitory potency depends on the chain length of the ubiquinol substrate and is higher with Q0C5 than with Q0C10, inhibition is pH-dependent
2,3,4-trimethoxy-5-methyl-6-decyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibition is pH-dependent
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
-
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
2-alkyl-3-hydroxy-1,4-naphthoquinone
-
-
2-heptyl-4-hydroxyquinoline N-oxide
2-Heptyl-4-hydroxyquinoline-N-oxide
2-Iodo-6-isopropyl-3-methyl-2',2,4'-trinitrodiphenyl ether
-
-
2-nonyl-4-hydroxyquinoline N-oxide
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
2-nonyl-4-hydroxyquinoline-N-oxide
-
-
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[3H]azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
-
azidoQ
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-ethyl-N-(4-hydroxyphenyl)benzenesulfonamide
-
-
4-tert-butyl-N-(2-hydroxyphenyl)benzenesulfonamide
-
-
4-tert-butyl-N-(3-hydroxyphenyl)benzenesulfonamide
-
-
4-tert-butyl-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
-
-
4-tert-butyl-N-(4-hydroxyphenyl)benzenesulfonamide
-
-
4-tert-butyl-N-(8-hydroxyquinolin-5-yl)benzenesulfonamide
-
-
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-(phenylamino)-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
5-(biphenyl-4-ylsulfonamido)-2-hydroxybenzoic acid
-
-
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
i.e. famoxadone, noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole
6-((1-hydroxynaphthalen-4-ylamino)dioxysulfone)-2H-naphtho[1,8-bc]thiophen-2-one
-
-
antimycin A1
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
antimycin-A
-
strong inhibition of Q-cycle bypass reactions
AS2077715
-
selective inhibitor, IC50 of 0.9 ng/ml
azoxystrobin
-
noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
methoxyacrylate-stilbene
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N-(3-chloro-4-hydroxyphenyl)biphenyl-4-sulfonamide
-
-
N-(3-fluoro-4-hydroxyphenyl)biphenyl-4-sulfonamide
-
-
N-(4-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
-
-
N-(4-hydroxyphenyl)-4-methylbenzenesulfonamide
-
-
N-(4-hydroxyphenyl)biphenyl-4-sulfonamide
-
-
N-(4-hydroxyphenyl)naphthalene-2-sulfonamide
-
-
N-(4-hydroxyphenyl)quinoline-8-sulfonamide
-
-
N-(5-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
-
-
N-(7-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
-
-
N-(8-hydroxyquinolin-5-yl)biphenyl-4-sulfonamide
-
-
n-2-heptyl-1-hydroxyquinoline N-oxide
-
-
n-alkyl-6-hydroxy-4,7-dioxobenzothiazole
-
length of side chain 7-15 carbon atoms
n-heptyl-4-hydroxyquinoline-N-oxide
-
-
potassium 4-(biphenyl-4-ylsulfonamido)phenolate
-
-
undecyl-hydroxy-dioxobenzoxythiazole
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2-heptyl-4-hydroxyquinoline N-oxide
-
-
2-heptyl-4-hydroxyquinoline N-oxide
-
-
2-heptyl-4-hydroxyquinoline N-oxide
-
-
2-Heptyl-4-hydroxyquinoline-N-oxide
-
-
2-Heptyl-4-hydroxyquinoline-N-oxide
-
-
5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole
-
competitive, structure of the enzyme with the hydroxyquinone anion Qo site inhibitor bound, binding mechanism
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
-
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
-
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
Antimycin
-
-
396001, 439944, 439947, 439948, 439950, 439952, 439962, 439995, 440005, 440027, 440035, 657683
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
Antimycin
-
effective inhibitor
Antimycin
-
inhibits ubiquinone reduction at the Qc site of the enzyme
Antimycin
-
highly reduces the rate of cytochrome c1
Antimycin
-
due to half-of-sites mechanism of the enzyme, 1 inhibitor molecule per enzyme complex dimer is sufficient for inhibition, center N inhibitor
Antimycin
-
center N inhibitor, acts at the Qn site of the bc1 complex, binding mode differing from ilicicolin
Antimycin
-
a Qn site inhibitor
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
antimycin A
-
-
antimycin A
-
most potent inhibitor
antimycin A
-
inhibits the enzyme complex and blocks the cell differentiation, inhibition mechanism
antimycin A
-
binds to center N sites, irreversible conformational change occurrs upon SQ formation in the active monomer
atovaquone
-
-
atovaquone
-
an anti-malarial agent that specifically targets the cytochrome bc1 complex and inhibits parasite respiration in vivo, mutants Y279S, Y279C, and L282V are resistant to the inhibition, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes
famoxadone
-
reversible, tight-binding, non-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
funiculosin
-
weak
funiculosin
-
similar to ilicicolin
funiculosin
-
a Qn site inhibitor
ilicicolin H
-
weak inhibitor, IC50 is above 100 nM
ilicicolin H
-
weak inhibitor
ilicicolin H
-
center N inhibitor
ilicicolin H
-
center N inhibitor, the antibiotic substance acts at the Qn site of the bc1 complex, isolated from the fungus Cylindrocladium iliciola strain MFC-870, binding mode differing from antimycin, effects on kinetics
ilicicolin H
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
ilicicolin H
-
potent inhibitor. S20T, Q22E, Q22T and L198F mutations in the yeast bc1 complex conferr resistance to ilicicolin H
menaquinol
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
reversible, tight-binding, mixed-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
methoxyacrylate stilbene
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
methoxyacrylate stilbene
-
-
Myxothiazol
-
-
Myxothiazol
-
inhibits ubiquinone reduction at the Qz site of the enzyme
Myxothiazol
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
Stigmatellin
-
-
Stigmatellin
-
binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition
Stigmatellin
species-specific binding of the inhibitor, binding structure and mechanism, overview
Stigmatellin
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
Stigmatellin
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
Stigmatellin
-
binds to center P sites
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
-
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
-
undecyl-hydroxy-dioxobenzoxythiazole
-
-
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
-
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His267, Lys269, and Asp254
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His268, Lys270, and Asp253
Zn2+
-
crystalline chicken bc1 complex specifically binds Zn2+ ions at two identical sites or one per monomer in the dimer. Zinc binding occurs close to the QP site and is likely to be the reason for the inhibitory effect on the activity of bc1 observable during zinc titration. The Zn2+ ion binds to a hydrophilic area between cytochromes b and c1 and is coordinated by GgH212 of cyt c1, GgH268, GgD253, and GgE255 of cyt b, and might interfere with the egress of protons from the QP site to the intermembrane aqueous medium. No Zn2+ is bound at the zinc binding motif of the putative MPP active site of core-1 and core-2 for chicken bc1 after prolonged soaking
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Zinc binds five to six N or O atoms
additional information
-
structure determination of the inhibitor binding site Qi, located near the matrix side of the membrane bilayer
-
additional information
-
ubiquinol cannot act as inhibitor
-
additional information
-
insensitive to N',N'-dicyclohexylcarbodiimide
-
additional information
-
-
-
additional information
-
inhibitor binding at the quinone reduction Qi side or the quinol oxidation Qo side
-
additional information
-
ubiquinol cannot act as inhibitor
-
additional information
-
resistant to classical inhibitors like myxothiazol, stigmatellin and antimycin
-
additional information
-
the rate of cytochrome c1 is highly reduced in absence of ubiquinone
-
additional information
-
inhibition and inhibitor binding mechanisms
-
additional information
-
design, synthesis, and kinetic evaluation of 3-(phenylamino)oxazolidine-2,4-diones as potent cytochrome bc1 complex inhibitors, overview
-
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0.00001593
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001517
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.00005998
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.00000944 - 0.001049
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
0.00001879
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.00005792
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.00002404
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
Sus scrofa
-
pH 7.4, 23°C
0.02
4-ethyl-N-(4-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.008
4-tert-butyl-N-(2-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.098
4-tert-butyl-N-(3-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-tert-butyl-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.005
4-tert-butyl-N-(4-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-tert-butyl-N-(8-hydroxyquinolin-5-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
Sus scrofa
-
above, pH 7.4, 23°C
0.005312
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
Sus scrofa
-
pH 7.4, 23°C
0.0002752
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
Sus scrofa
-
pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-(phenylamino)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.02
5-(biphenyl-4-ylsulfonamido)-2-hydroxybenzoic acid
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.00002376
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.0000482 - 0.000142
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
0.00006326
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.005
6-((1-hydroxynaphthalen-4-ylamino)dioxysulfone)-2H-naphtho[1,8-bc]thiophen-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
antimycin A
Roseobacter denitrificans
-
-
0.000327
atovaquone
Plasmodium berghei
-
at pH 8.0 and 25°C
0.0004347 - 0.000527
azoxystrobin
0.000012
ilicicolin H
Saccharomyces cerevisiae
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
0.00004
Myxothiazol
Roseobacter denitrificans
-
-
0.02
N-(3-chloro-4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(3-fluoro-4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)-4-methylbenzenesulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.0025
N-(4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)naphthalene-2-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)quinoline-8-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(5-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(7-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(8-hydroxyquinolin-5-yl)biphenyl-4-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.005
potassium 4-(biphenyl-4-ylsulfonamido)phenolate
Homo sapiens
-
pH and temperature not specified in the publication
0.00000944
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.000337
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.001049
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.0000482
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
Sus scrofa
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.000142
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
Sus scrofa
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.0004347
azoxystrobin
Sus scrofa
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.000527
azoxystrobin
Sus scrofa
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
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malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity, which is inactive in bovine cells, but can be activated through detergents treatment
metabolism
-
the bc1 complex is a functional substituent of CymA in nitrate/nitrite respiration
physiological function
-
reaction mechanism of superoxide generation by bc1, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
the bc1 complex, is the enzyme in the respiratory chain of mitochondria responsible for the transfer reducing potential from ubiquinol to cytochrome c coupled to the movement of charge against the electrostatic potential across the mitochondrial inner membrane. The complex is also implicated in the generation of reactive oxygen species under certain conditions and is thus a contributor to cellular oxidative stress
physiological function
-
the cytochrome bc1 complex is an essential energy transduction electron transfer complex in photosynthetic bacteria. This complex catalyzes the electron transfer from ubiquinol to cytochrome c (or c2) with concomitant generation of a proton gradient and membrane potential for ATP synthesis by the ATP synthase complex
physiological function
the respiratory cytochrome bc1 complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of protonmotive force which fuels ATP synthesis
physiological function
-
the enzyme contributes to the loss-of-cardioprotection model induced by long-term diazoxide treatment and plays a role in delayed cardioprotection
physiological function
-
the overexpression of ubiquinol-cytochrome c reductase core protein 1 can protect H9c2 cardiac cells against simulated ischemia/reperfusion
physiological function
ubiquinolcytochrome c reductase binding protein induces angiogenesis in vitro and in vivo
physiological function
simulation of the enzyme kinetics under a wide range of conditions using a functional dimer model. The model consists of six electronic states characterized by the number of electrons deposited on the complex and is fully reversible. In normal steady-state conditions, only a single Qp site in the dimer is operational per quinol oxidation. The quinone pool is mostly oxidized under normal physiological operation but can switch to a more reduced state when reverse electron transport conditions are in place
physiological function
-
subunit ActE of alternative complex III functions as a direct electron donor to the cytochrome c aa3 oxygen reductase. The reduction potential of ActE is +165 mV, at pH 7.5
physiological function
-
subunit ActE of alternative complex III functions as a direct electron donor to the cytochrome c aa3 oxygen reductase. The reduction potential of ActE is +165 mV, at pH 7.5
-
additional information
-
mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme complex from Phaeospirillum molischianum shows a more random organization and slower reaction center turnover compared to the enzyme complex from Rhodobacter sphaeroides
additional information
-
mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme shows a highly organized arrangement of light harvesting and reaction center complexes and fast reaction center electron transfer turnover. Cytochrome bc1 or ATPase complexes are localized in membrane domains distinct from the flat regions. Modeling of subunit IV into the cytochrome bc1 complex
additional information
-
model of the bc1 complex for mammalian mitochondria incorporating the major redox centers near the Qo- and Qi-site of the enzyme, and including the pH-dependent redox reactions, overview. The model consists of six distinct states characterized by the mobile electron distribution in the enzyme
additional information
structural diversity in the cytochrome c1 surface facing the iron-sulfur protein domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. Modelling of the electron transfer complex with membrane-anchored cytochrome c552, the natural substrate
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
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11200
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
114000
-
calculated from subunit composition
121000
-
calculation from cytochrome content
12300
-
subunit VI, SDS-PAGE
12700
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
13345
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
13380
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
134000
-
sedimentation equilibrium
139000
-
diffusion coefficient/sedimentation coefficient
18000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
19000
-
FeS-protein, SDS-PAGE
207500
-
summation of protein components
21000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
21540
-
Rieske iron sulfur protein, apoprotein, amino acid sequence
216000
-
bc1 subcomplex, SDS-PAGE
21608
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
21630
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
21710
-
Rieske iron sulfur protein, holoprotein, including [Fe2-S2] cluster, amino acid sequence
22400
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
22500
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
238000
-
estimated from a specific cytochrome c1 content of 4.2 nmol/mg protein
240000 - 250000
-
from concentration of prosthetic groups
241100
-
total mass of protein moiety
242000
-
minimum molecular weight calculated from stoichiometry
243300
-
complete enzyme monomer, amino acid composition
248000
-
bc1 complex, SDS-PAGE
262000 - 288000
-
light-scattering measurement
268000
-
cytochrome c1 content
27000
-
cytochrome b, SDS-PAGE
27285
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
27350
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
27900
-
cytochrome c1, SDS-PAGE
290000
-
from subunit composition
32600
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
33000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
34100
-
His-tagged cyt c1, SDS-PAGE
400000
-
ultracentrifugation sedimentation velocity
40100
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
40800
-
His-tagged cyt b, SDS-PAGE
42500
-
cytochrome b, calculated from amino acid sequence
42588
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
42727
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
43700
-
cytochrome b, SDS-PAGE
44000 - 48000
-
core protein, SDS-PAGE
440000
-
from hydrodynamic measurements
46000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
46520
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
46808
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
48960
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
49200
-
core protein I, amino acid sequence
49209
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
500000
-
analytical ultracentrifugation
50240
-
core protein, calculated from amino acid composition
60000 - 68000
-
cytochrome c1
6519
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
7326
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
7955
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
8053
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
88400
-
calculation from subunit composition, assuming stoechiometry of 1:1:1
9174
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
9261
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
9507
-
amino acid sequence
9588
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
10000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
11000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
11000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
11000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
11000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
11000
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
11000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
11000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
11500
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
11500
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
12000
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
12000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
12000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
12000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
12000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
13000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
13000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
13000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
13000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
13400
-
Q-binding protein, SDS-PAGE
13400
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
13400
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
14000
-
QP-C, ubiquinone binding protein, amino acid sequence
14000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
14000
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
14000
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
14000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
14000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
14000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
14000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
14000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
14000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
15000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
15000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
15000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
16000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
16000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
16000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
17000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
17000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
17000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
17000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
20000
-
-
20000
-
Rieske iron sulfur protein
20000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
20000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
20000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
200000
-
protein determination
200000
-
minimum molecular weight, calculated from heme contents
22000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
22000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
23000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
23000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
23000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
24000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
24000
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
24000
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
24000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
24000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
24000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
24000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
24000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
25000
-
iron-sulfur protein [Fe2-S2], SDS-PAGE
25000
-
iron-sulfur protein [Fe2-S2], SDS-PAGE
25000
-
iron-sulfur protein [Fe2-S2], SDS-PAGE
25000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
25000
-
1 * 40000 + 1 * 34000 + 1 * 25000
25000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
25000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
25000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
25000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
25000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
25000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
250000
-
ultracentrifugation
250000
-
sedimentation velocity
250000
-
from subunit composition
250000
-
2 * 250000, SDS-PAGE
26000
-
gel filtration
26000
-
iron-sulfur protein, SDS-PAGE
28000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
28000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
285000
-
-
285000
-
from concentration of prosthetic groups
29000
-
cytochrome c1, SDS-PAGE
29000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
29000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
29000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
29000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
30000
-
cytochrome c, SDS-PAGE
30000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
30000
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
30000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
30000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
30000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
30000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
31000
-
-
31000
-
cytochrome c1, SDS-PAGE
31000
-
cytochrome c and cytochrome b, SDS-PAGE
31000
-
cytochrome c and cytochrome b, SDS-PAGE
31000
-
cytochrome b monomer, SDS-PAGE
31000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
31000
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
31000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
31000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
31000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
32000
-
cytochrome b, SDS-PAGE
32000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
32000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
34000
-
1 * 40000 + 1 * 34000 + 1 * 25000
34000
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
34000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
34000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
34000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
35000
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
35000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
39000
-
cytochrome b
39000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
40000
-
subunit II, SDS-PAGE
40000
-
1 * 40000 + 1 * 34000 + 1 * 25000
40000
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
40000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
40000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
40000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
40000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
43000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
43000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
43000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
43000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
44000
-
-
44000
-
core protein, SDS-PAGE
44000
-
c1 subcomplex, SDS-PAGE
44000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
44000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
44000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
45000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
45000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
45000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
45000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
45000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
45000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
45000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
45000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
45000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
47000
-
core protein I, SDS-PAGE
47000
-
core II, SDS-PAGE
47000
-
core protein 2, SDS-PAGE
47000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
47000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
47000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
47000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
47000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
48000
-
cytochrome b, SDS-PAGE
48000
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
49000
-
core I, SDS-PAGE
49000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
49000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
50000
-
core protein 1, SDS-PAGE
50000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
52000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
52000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
52000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
550000
-
-
550000
-
from hydrodynamic measurements
6000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
6000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
6000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
62000
-
-
62000
-
dimeric cytochrome b
6400
-
-
6400
-
ISP-associated protein, SDS-PAGE
6400
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
6400
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
7200
-
-
7200
-
cytochrome c1-associated protein, SDS-PAGE
7200
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
8000
-
-
8000
-
subunit IX, SDS-PAGE
8000
-
DCCD-binding protein, SDS-PAGE
8000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
8000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
8000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
8000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
8000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
9000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
9000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
9000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
9000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
9175
-
-
9175
-
heme-not containing protein, amino acid sequence
9200
-
hinge protein, SDS-PAGE
9200
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
9200
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
9500
-
-
9500
-
subunit ubiquinone-binding protein QPc, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dodecamer
-
subunits I, II, III, IV, V, VI, VIIA, VIIB, VIII, IX, X and XI
?
x * 43000, PTD-enzyme fusion protein, SDS-PAGE
?
-
x * 18000, SDS-PAGE of subunit ActE, truncated protein lacking 26 amino acid signal sequence
?
-
x * 18000, SDS-PAGE of subunit ActE, truncated protein lacking 26 amino acid signal sequence
-
dimer
-
-
dimer
-
each monomeric unit consists of 9 different subunits
dimer
-
subunit I: 50000 Da, subunit II: 45000 Da, Rieske iron-sulfur protein 22000 Da and for subunits from 14000-8000 Da
dimer
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
dimer
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
-
dimer
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer
dimer
-
2 * 250000, SDS-PAGE
dimer
-
complex composition, binding structure of cytochromes, crystal structure, overview
dimer
-
cytochrome bc1 complex, electron transfer complex structure
dimer
-
dimeric cytochrome bc1 complex, structure overview
heptamer
-
-
heptamer
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
heptamer
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
heptamer
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
heptamer
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
heptamer
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
nonamer
-
-
nonamer
-
9 subunits range in size from 7200-44000 Da
octamer
-
-
octamer
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
octamer
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
octamer
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
octamer
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
octamer
-
composed of 8 different subunits with molecular weights ranging from 11-44 kDa
octamer
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
oligomer
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
oligomer
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
oligomer
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
pentamer
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
-
-
tetramer
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
tetramer
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
tetramer
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
tetramer
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
-
tetramer
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
-
trimer
-
-
trimer
-
1 * 40000 + 1 * 34000 + 1 * 25000
trimer
-
1 * 40000 + 1 * 34000 + 1 * 25000
-
trimer
-
1 * 62000 + 1 * 39000 + 1 * 20000
trimer
-
1 * 62000 + 1 * 39000 + 1 * 20000, cytochrome c1, cytochrome b, Rieske-type iron-sulfur protein, SDS-PAGE
trimer
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
trimer
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
-
trimer
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
undecamer
-
-
undecamer
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
undecamer
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
undecamer
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
additional information
-
enzyme complex subunit composition and stoichiometry, subunits of 14, 21, 25, 32, 40, and 55 kDa, overview
additional information
-
enzyme is part of the mitochondrial cytochrome bc1 complex
additional information
-
structure modeling and analysis, overview
additional information
-
separation of multienzyme complex III components, mass spectrometral analysis, complex composition, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
the Rhodobacter sphaeroides complex contains four protein subunits: three core subunits and one supernumerary subunit
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
separation of multienzyme complex III components, mass spectrometral analysis, complex composition, overview
additional information
-
spectroscopic enzyme complex composition analysis, structural changes upon cofactor or substrate binding, overview
additional information
-
3 catalytic subunits
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
enzyme complex is a dimer of oligomeric complexes with 11 subunits, composition analysis by mass spectrometry, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
interaction analysis between monomers of the dimeric enzyme complex
additional information
-
modeling the variations in cytochrome b structure with the mutated bc1 complexes
additional information
-
secondary structure of yeast cytochrome b and a view of center N, overview
additional information
-
blue-native PAGE analysis: supercomplex composed of dimeric complex III and two copies of monomeric complex IV, supercomplex composed of dimeric complex III and one copy of monomeric complex IV, dimeric complex III
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
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