Nitrite reductase (cytochrome; ammonia-forming)

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume 24)

Nomenclature

EC number

1.7.2.2

Systematic name

ammonia:ferricytochrome-c oxidoreductase

Recommended name

nitrite reductase (cytochrome; ammonia-forming)

Synonyms

NiR cytochrome C552 <6> [6]

ammonia-forming cytochrome c nitrite reductase <5> [5]

cytochrome c NiR <6> [6]

cytochrome c nitrite reductase

cytochrome c552 <1> [1]

hexaheme c-type cytochrome <2> [2]

multiheme nitrite reductase

CAS registry number

37256-41-0

Keywords

Nitric Oxide Reaction Type Nitrite Reductase Covalent Attachment Inhibitor Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Kajie, S.; Anraku, Y.: Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase. Eur. J. Biochem., 154, 457–463 (1986)PubMedCrossRefGoogle Scholar
  2. [2]
    Liu, M.C.; Bakel, B.W.; Liu, M.Y.; Dao, T.N.: Purification of Vibrio fischeri nitrite reductase and its characterization as a hexaheme c-type cytochrome. Arch. Biochem. Biophys., 262, 259–265 (1988)PubMedCrossRefGoogle Scholar
  3. [3]
    Einsle, O.; Stach, P.; Messerschmidt, A.; Simon, J.; Kroger, A.; Huber, R.; Kroneck, P.M.H.: Cytochrome c nitrite reductase from Wolinella succinogenes structure at 1.6.ANG. resolution, inhibitor binding, and heme-packing motifs. J. Biol. Chem., 275, 39608–39616 (2000)PubMedCrossRefGoogle Scholar
  4. [4]
    Einsle, O.; Stach, P.; Messerschmidt, A.; Klimmek, O.; Simon, J.; Kroger, A.; Kroneck, P.M.: Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes. Acta Crystallogr. Sect. D, 58, 341–342 (2002)CrossRefGoogle Scholar
  5. [5]
    Schumacher, W.; Hole, U.; Kroneck, P.M.: Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties. Biochem. Biophys. Res. Commun., 205, 911–916 (1994)PubMedCrossRefGoogle Scholar
  6. [6]
    Pereira, I.A.C.; LeGall, J.; Xavier, A.V.; Teixeira, M.: Characterization of a heme c nitrite reductase from a non-ammonifying microorganism, Desulfovibrio vulgaris Hildenborough. Biochim. Biophys. Acta, 1481, 119–130 (2000)PubMedGoogle Scholar
  7. [7]
    Costa, C; Moura, J.J.; Moura, I.; Wang, Y.; Huynh, B.H.: Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. J. Biol. Chem., 271, 23191–23196 (1996)PubMedCrossRefGoogle Scholar
  8. [8]
    Eaves, D.J.; Grove, J.; Staudenmann, W.; James, P.; Poole, R.K.; White, S.A.; Griffiths, I.; Cole, J.A.: Involvement of products of the nrfEFG genes in the covalent attachment of heme c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli. Mol. Microbiol., 28, 205–216 (1998)PubMedCrossRefGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2005

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