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Literature summary extracted from

  • Judd, E.T.; Youngblut, M.; Pacheco, A.A.; Elliott, S.J.
    Direct electrochemistry of Shewanella oneidensis cytochrome c nitrite reductase: evidence of interactions across the dimeric interface (2012), Biochemistry, 51, 10175-10185.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.2.2 nitrite substrate inhibition Shewanella oneidensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.2 0.054
-
 nitrite pH 8.3, 20°C Shewanella oneidensis

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.2 Shewanella oneidensis Q8EAC7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.2 additional information protein film voltammetry shows that all detected electron transfer steps are one-electron in nature. Enzyme displays substrate inhibition during nitrite turnover and negative cooperativity during hydroxylamine turnover Shewanella oneidensis ?
-
 ?
1.7.2.2 nitrite + reduced + acceptor
-
 Shewanella oneidensis NH3 + oxidized acceptor + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.7.2.2 NrfA
-
 Shewanella oneidensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.2 7
-
 nitrite pH 8.3, 20°C Shewanella oneidensis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.7.2.2 18
-
 nitrite pH 8.3, 20°C Shewanella oneidensis