IntEnz

EC 1.7.2.2 - Nitrite reductase (cytochrome; ammonia-forming)

IntEnz Enzyme Nomenclature
EC 1.7.2.2

Names

Reaction

• 13089 [IUBMB]
  6

  [Fe(III)cytochrome c]

  [Fe(III)cytochrome c]

  GENERIC:14399

  Is ROOT: no
  ROOT compound: GENERIC:9753

  Number of residues: 1

  Fe3+ Fe(3+) Name origin: UniProt - CHECKED (C) CHEBI:29034 Formula: Fe Charge: 3 Position: undefined ChEBI compound status: CHECKED (C)

  +

  2

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  NH₄⁺

  NH4(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:28938

  Formula: H4N
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  =

  6

  [Fe(II)cytochrome c]

  [Fe(II)cytochrome c]

  GENERIC:10350

  Is ROOT: no
  ROOT compound: GENERIC:9753

  Number of residues: 1

  Fe2+ Fe(2+) Name origin: UniProt - CHECKED (C) CHEBI:29033 Formula: Fe Charge: 2 Position: undefined ChEBI compound status: CHECKED (C)

  +

  8

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  nitrite

  nitrite

  Name origin: UniProt - CHECKED (C)

  CHEBI:16301

  Formula: NO2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

Cofactors

• heme
• Ca²⁺

Comments:

Found as a multiheme cytochrome in many bacteria. The enzyme from Escherichia coli contains five hemes c and requires Ca²⁺. It also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide.

Links to other databases

References

1. Einsle, O., Messerschmidt, A., Stach, P. Bourenkov, G.P., Bartunik, H.D., Huber, R. and Kroneck, P.M.H.
   Structure of cytochrome c nitrite reductase.
   Nature 400: 476-480 (1999). [PMID: 10440380]

[EC 1.7.2.2 created 2001]