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Literature summary for 1.19.6.1 extracted from

  • Duyvis, M.G.; Wassink, H.; Haaker, H.
    Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle (1998), Biochemistry, 37, 17345-17354.
    View publication on PubMed
Search for more literature for 1.19.6.1

Metals/Ions

Metals/Ions Comment Organism Structure
Iron enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex Azotobacter vinelandii
Mg2+ required for ATP hydrolysis Azotobacter vinelandii
Molybdenum enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex Azotobacter vinelandii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000
-
 nitrogenase MoFe protein component Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP Azotobacter vinelandii enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate limiting step of the cycle 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Reaction

Reaction Comment Organism Reaction ID
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate enzyme is composed of 2 metalloproteins: Fe protein and MoFe protein which are assumed to associate and dissociate to transfer a single electron to the substrates Azotobacter vinelandii
a
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate mechanism, Fe protein cycle Azotobacter vinelandii
a
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate enzyme complex dissociation and association kinetics Azotobacter vinelandii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate-limiting step of the cycle Azotobacter vinelandii 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate i.e. flavodoxin semiquinone ?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP slow enzyme Azotobacter vinelandii 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate i.e. flavodoxin semiquinone ?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP intermediate is a flavodoxin hydroquinone Azotobacter vinelandii 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate i.e. flavodoxin semiquinone ?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate limiting step of the cycle Azotobacter vinelandii 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
 ?
dithionite + H+ + N2 + ATP
-
 Azotobacter vinelandii ?
-
 ?
flavodoxin hydroquinone + H+ + N2 + ATP + H2O
-
 Azotobacter vinelandii ?
-
 ?
additional information dithionite can serve as reductant in vitro Azotobacter vinelandii ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * alpha-beta-monomer Azotobacter vinelandii
More alpha-beta-monomer of the FeMo protein consists of the FeMo cofactor FeMoco with the substrate reduction site and the P-cluster Azotobacter vinelandii
More enzyme is composed of 2 metalloproteins: Fe protein and MoFe protein which are assumed to associate and dissociate to transfer a single electron to the substrates Azotobacter vinelandii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
400
-
 flavodoxin hydroquinone before and after reduction of the nitrogenase complex relative slow reactions take place, which limits the rate of the Fe protein cycle Azotobacter vinelandii