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Literature summary for 1.18.6.1 extracted from

  • Scott, A.D.; Pelmenschikov, V.; Guo, Y.; Yan, L.; Wang, H.; George, S.J.; Dapper, C.H.; Newton, W.E.; Yoda, Y.; Tanaka, Y.; Cramer, S.P.
    Structural characterization of CO-inhibited Mo-nitrogenase by combined application of nuclear resonance vibrational spectroscopy, extended X-ray absorption fine structure, and density functional theory new insights into the effects of CO binding and the (2014), J. Am. Chem. Soc., 136, 15942-15954 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H195Q the mutant shows stronger nuclear resonance vibrational spectroscopy features in the Fe-CO region compared to wild type enzyme Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
CO
-
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
-
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii P07328 and P07329 alpha and beta chains
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Mo-nitrogenase
-
Azotobacter vinelandii
N2ase
-
Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Azotobacter vinelandii
iron-molybdenum cofactor Mo-7Fe-9S-Ci-homocitrate Azotobacter vinelandii