Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.7.2.2 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

Inhibitors Comment Organism Structure
nitrite substrate inhibition Shewanella oneidensis

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Shewanella oneidensis Q8EAC7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
nitrite + reduced + acceptor
-
Shewanella oneidensis NH3 + oxidized acceptor + H2O
-
?

Synonyms

Synonyms Comment Organism
NrfA
-
Shewanella oneidensis

Turnover Number [1/s]

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

Ki Value [mM]

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