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Literature summary extracted from

  • Fisher, K.; Dilworth, M.J.; Kim, C.H.; Newton, W.E.
    Azotobacter vinelandii nitrogenases with substitutions in the FeMo-cofactor environment of the MoFe protein: effects of acetylene or ethylene on interactions with H+, HCN, and CN- (2000), Biochemistry, 39, 10855-10865.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.18.6.1 C2H2 enhances the CH4 production but not NH3 production from CN-, wild-type enzyme Azotobacter vinelandii

Protein Variants

EC Number Protein Variants Comment Organism
1.18.6.1 H195N alphaHis195 of MoFe protein, shows 59% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition, NH3 production decreased much less Azotobacter vinelandii
1.18.6.1 H195Q alphaHis195 of MoFe protein, shows 159% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition Azotobacter vinelandii
1.18.6.1 Q191K alphaGln191 of MoFe protein, shows 6% activity compared to wild-type, substrate CN-, not affected by addition of C2H2 Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 CO inhibition of CH4 and NH3 production from CN- Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.6.1 0.45
-
 CH4 mutant H195Q Azotobacter vinelandii
1.18.6.1 1.6
-
 CH4 wild-type Azotobacter vinelandii
1.18.6.1 4.5
-
 CH4 mutant H195N Azotobacter vinelandii
1.18.6.1 12
-
 CH4 mutant Q191K Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron
-
 Azotobacter vinelandii
1.18.6.1 Molybdenum mol Mo per mol MoFeprotein: wild-type and mutant H195Q 1.9, mutant H195N and Q191K 0.9 Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Azotobacter vinelandii
-
 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.6.1 wild-type and mutants H195Q, H195N, Q191K Azotobacter vinelandii

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.6.1 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Azotobacter vinelandii 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + CN- + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.6.1 30
-
 assay at Azotobacter vinelandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.6.1 7.4
-
 assay at Azotobacter vinelandii