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Literature summary extracted from

  • Lee, H.I.; Sorlie, M.; Christiansen, J.; Yang, T.C.; Shao, J.; Dean, D.R.; Hales, B.J.; Hoffman, B.M.
    Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO (2005), J. Am. Chem. Soc., 127, 15880-15890.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
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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 SEPR1 intermediate formed during turnover of the nitrogenase alpha-195Gln MoFe protein with C2H2 in H2O buffers, is a product complex with C2H4 bound as a ferracycle to a single Fe of the FeMo-cofactor active site. CO bridges two Fe of lo-Co, while the C2H4 of SEPR1 binds to one of these. Correlation with Lowe-Thorneley En kinetic state Azotobacter vinelandii