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Literature summary for 1.18.6.1 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
Search for more literature for 1.18.6.1

Activating Compound

Activating Compound Comment Organism Structure
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

Protein Variants Comment Organism
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

Metals/Ions Comment Organism Structure
Mg2+ required Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N2 + 8 e- + 8 H+ + 16 ATP Azotobacter vinelandii
-
 2 NH3 + H2 + 16 ADP + 16 phosphate
-
 ir

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N2 + 8 e- + 8 H+ + 16 ATP
-
 Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
-
 ir
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

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