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Literature summary for 1.18.6.1 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
Search for more literature for 1.18.6.1

Activating Compound

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + H+ + N2 + ATP + H2O Azotobacter vinelandii biological nitrogen fixation oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ir

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
 molybdenum-dependent enzyme variant
-

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylene + ?
-
 Azotobacter vinelandii ethylene + ?
-
 ?
reduced ferredoxin + H+ + N2 + ATP + H2O biological nitrogen fixation Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ir
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

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