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Literature summary extracted from

  • Seefeldt, L.C.; Dance, I.G.; Dean, D.R.
    Substrate interactions with nitrogenase: Fe versus Mo (2004), Biochemistry, 43, 1401-1409.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.18.6.1 additional information H2 generation activates N2 binding Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 Acetylene noncompetitive inhibition of N2 reduction Azotobacter vinelandii
1.18.6.1 CO
-
 Azotobacter vinelandii
1.18.6.1 H2 competitive inhibition of N2 binding Azotobacter vinelandii
1.18.6.1 N2 competitive inhibition of acetylene reduction Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, 1 of 2 different models proposes one or more Fe atoms in the Mo cofactor to be responsible for substrate binding Azotobacter vinelandii
1.18.6.1 Molybdenum enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, where X can be an N atom, 1 of 2 different models proposes molydenum as the substrate binding partner in the active site 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 reduced ferredoxin + H+ + N2 + ATP + H2O Azotobacter vinelandii biological nitrogen fixation oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
 molybdenum-dependent enzyme variant
-

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 theoretical mechanisms of substrate binding to molybdenum or iron in the FeMo cofactor, modeling Azotobacter vinelandii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 acetylene + ?
-
 Azotobacter vinelandii ethylene + ?
-
 ?
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP + H2O biological nitrogen fixation Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ir
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP + H2O in absence of N2 or other substrates, the electron flow is directed towards proton reduction Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ir

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 ATP
-
 Azotobacter vinelandii
1.18.6.1 Ferredoxin
-
 Azotobacter vinelandii
1.18.6.1 iron-molybdenum cofactor enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, structure, redox status, part of the MoFe protein Azotobacter vinelandii