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Literature summary for 1.7.2.1 extracted from

  • Zhao, Y.; Lukoyanov, D.A.; Toropov, Y.V.; Wu, K.; Shapleigh, J.P.; Scholes, C.P.
    Catalytic function and local proton structure at the type 2 copper of nitrite reductase: the correlation of enzymatic pH dependence, conserved residues, and proton hyperfine structure (2002), Biochemistry, 41, 7464-7474.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type, D129A, D129N, H287A, I289A and I289V mutant enzymes in Escherichia coli Cereibacter sphaeroides

Protein Variants

Protein Variants Comment Organism
D129A low activity Cereibacter sphaeroides
D129N low activity Cereibacter sphaeroides
H287A very low activity Cereibacter sphaeroides
I289A activity comparable to wild-type Cereibacter sphaeroides
I289V activity comparable to wild-type Cereibacter sphaeroides
M182T activity comparable to wild-type Cereibacter sphaeroides

Metals/Ions

Metals/Ions Comment Organism Structure
copper
-
Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + ferrocytochrome c
-
Cereibacter sphaeroides nitric oxide + H2O + ferricytochrome c
-
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