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 to perform the reduction of nitrite to ammonium  in a six-electron transfer reaction <ref>pmid 14511372</ref>
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 <ref>pmid 14511372</ref> <ref>pmid 8798514</ref>


</StructureSection>     
</StructureSection>     
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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.
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 a pentahemic subunit of 61 kDa which is strongly bound to its physiological electron donor, a smaller hydrophobic polypeptide tetrahemic of 19 kDa, composed of 4 c-types hemes; in vitro, the protein complexes associate each other forming huge aggregates (min. 890 kDa).
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).


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<references/>

Revision as of 11:26, 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 to perform the reduction of nitrite to ammonium in a six-electron transfer reaction [1] [2]



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. 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

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