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Literature summary extracted from

  • Roth, L.E.; Nguyen, J.C.; Tezcan, F.A.
    ATP- and iron-protein-independent activation of nitrogenase catalysis by light (2010), J. Am. Chem. Soc., 132, 13672-13674.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.18.6.1 light light-driven activation of the molybdenum-iron-protein, MoFeP, of nitrogenase for substrate reduction is independent of ATP hydrolysis and the iron-protein, FeP, binding structure and mechanism, overview Azotobacter vinelandii

Protein Variants

EC Number Protein Variants Comment Organism
1.18.6.1 additional information a MoFeP variant labeled on its surface with a Ru-photosensitizer is shown to photocatalytically reduce protons and acetylene, most likely at its active site, FeMoco. The uncoupling of nitrogenase catalysis from ATP hydrolysis enables the study of redox dynamics within MoFeP and the population of discrete reaction intermediates, overview Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Mg2+ required 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 N2 + 8 e- + 8 H+ + 16 ATP Azotobacter vinelandii
-
 2 NH3 + H2 + 16 ADP + 16 phosphate
-
 ir

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 N2 + 8 e- + 8 H+ + 16 ATP
-
 Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
-
 ir
1.18.6.1 N2 + 8 e- + 8 H+ + 16 ATP cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
-
 ir

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 ATP
-
 Azotobacter vinelandii
1.18.6.1 FeMo cofactor binding structure and mechanism, overview Azotobacter vinelandii