CcNiR: Difference between revisions

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== Your Heading Here ('ccNiR') ==
== Your Heading Here ('ccNiR') ==
<StructureSection load='1oah' size='500' side='left' caption='CYTOCHROME C NITRITE REDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 (PDB entry [[1oah]])' scene=''>
<StructureSection load='1oah' size='500' side='left' caption='CYTOCHROME C NITRITE REDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 (PDB entry [[1oah]])' scene=''>
Cytochrome c nitrite reductase is a multicenter enzyme that uses a five-coordinated heme (<scene name='CcNiR/Fe/2'>heme iron</scene>) to perform the reduction of nitrite to ammonium  in a six-electron transfer reaction <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 20689707</ref>
Cytochrome c nitrite reductase is a multicenter enzyme that uses a five-coordinated heme (see <scene name='CcNiR/Fe/2'>heme iron</scene>) to perform the reduction of nitrite to ammonium  in a six-electron transfer reaction <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 20689707</ref>





Revision as of 11:57, 6 September 2012

Your Heading Here ('ccNiR')Your Heading Here ('ccNiR')

CYTOCHROME C NITRITE REDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 (PDB entry 1oah)

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Cytochrome c nitrite reductase is a multicenter enzyme that uses a five-coordinated heme (see ) to perform the reduction of nitrite to ammonium in a six-electron transfer reaction [1] [2] [3] [4]




Cytochrome c nitrite reductase is a multicenter enzyme that uses a five-coordinated heme to perform the reduction of nitrite to ammonium in a six-electron transfer reaction. In the sulfate reducing bacterium Desulfovibrio desulfuricans ATCC 27774, the enzyme is purified as a NrfA2NrfH complex that houses 14 hemes.

The catalytic reaction occurs at a high-spin (5-coordinated) heme that is located at the pentahemic subunit NrfA which is strongly bound to its physiological electron donor, the smaller hydrophobic polypeptide tetrahemic NrfH, composed of 4 c-types hemes; in vitro, the protein complexes associate each other forming huge aggregates (min. 890 kDa).

  1. Almeida MG, Macieira S, Goncalves LL, Huber R, Cunha CA, Romao MJ, Costa C, Lampreia J, Moura JJ, Moura I. The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774. Re-evaluation of the spectroscopic data and redox properties. Eur J Biochem. 2003 Oct;270(19):3904-15. PMID:14511372
  2. Cunha CA, Macieira S, Dias JM, Almeida G, Goncalves LL, Costa C, Lampreia J, Huber R, Moura JJ, Moura I, Romao MJ. Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA). J Biol Chem. 2003 May 9;278(19):17455-65. Epub 2003 Mar 4. PMID:12618432 doi:10.1074/jbc.M211777200
  3. Costa C, Moura JJ, Moura I, Wang Y, Huynh BH. Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. J Biol Chem. 1996 Sep 20;271(38):23191-6. PMID:8798514
  4. Silveira CM, Besson S, Moura I, Moura JJ, Almeida MG. Measuring the cytochrome C nitrite reductase activity-practical considerations on the enzyme assays. Bioinorg Chem Appl. 2010. pii: 634597. Epub 2010 Jun 22. PMID:20689707 doi:10.1155/2010/634597

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Gabriela Almeida, Michal Harel