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Literature summary for 1.18.6.1 extracted from

  • Bulen, W.A.; LeComte, J.R.
    Nitrogenase complex and its components (1972), Methods Enzymol., 24B, 456-470.
    View publication on PubMed

General Stability

General Stability Organism
nitrogenase complex is more stable than either the MoFe protein or the Fe protein alone Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
ADP above 5 mM Azotobacter vinelandii
ATP
-
Azotobacter vinelandii
Ca2+
-
Azotobacter vinelandii
CO
-
Azotobacter vinelandii
H2
-
Azotobacter vinelandii
hydrazine and derivatives Azotobacter vinelandii
additional information e.g. above 50 mM NaCl; high ionic strength inhibits Azotobacter vinelandii
phosphate above 30 mM Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
N2 with C2H2 Azotobacter vinelandii
0.3
-
C2H2
-
Azotobacter vinelandii
0.3
-
ATP with C2H2 Azotobacter vinelandii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can replace Mg2+, but is less effective Azotobacter vinelandii
Fe2+ can replace Mg2+, but is less effective Azotobacter vinelandii
Iron
-
Azotobacter vinelandii
Mg2+ Mg2+ required for MgATP complex Azotobacter vinelandii
Mn2+ can replace Mg2+, but is less effective Azotobacter vinelandii
Molybdenum
-
Azotobacter vinelandii
Ni2+ can replace Mg2+, but is less effective Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Azotobacter vinelandii
-
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Oxidation Stability

Oxidation Stability Organism
extreme O2 lability, susceptibility to O2 increases with purification, but is retarded in presence of MgCl2 Azotobacter vinelandii

Purification (Commentary)

Purification (Comment) Organism
-
Azotobacter vinelandii

Reaction

Reaction Comment Organism Reaction ID
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein Azotobacter vinelandii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Azotobacter vinelandii

Storage Stability

Storage Stability Organism
0°C, anaerobic conditions, FeMo protein stable Azotobacter vinelandii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
Azotobacter vinelandii 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
?
reduced ferredoxin + H+ + ATP in absence of other acceptors Azotobacter vinelandii oxidized ferredoxin + H2 + ADP + phosphate
-
?
reduced ferredoxin + H+ + CH3NC + ATP
-
Azotobacter vinelandii oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
?
reduced ferredoxin + H+ + N3- + ATP
-
Azotobacter vinelandii oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Azotobacter vinelandii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
Fe protein: cold labile Azotobacter vinelandii
22
-
Fe protein, half-life: 18 h Azotobacter vinelandii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
Azotobacter vinelandii