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Literature summary 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)

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

Protein Variants

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 copper
-
 Cereibacter sphaeroides

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

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