1gu6: Difference between revisions
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[[Category: periplasmic nitrite reductase]] | [[Category: periplasmic nitrite reductase]] | ||
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Revision as of 16:14, 30 October 2007
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STRUCTURE OF THE PERIPLASMIC CYTOCHROME C NITRITE REDUCTASE FROM ESCHERICHIA COLI
OverviewOverview
The crystal structure and spectroscopic properties of the periplasmic, penta-heme cytochrome c nitrite reductase (NrfA) of Escherichia coli are, presented. The structure is the first for a member of the NrfA subgroup, that utilize a soluble penta-heme cytochrome, NrfB, as a redox partner., Comparison to the structures of Wolinella succinogenes NrfA and, Sulfospirillum deleyianum NrfA, which accept electrons from a, membrane-anchored tetra-heme cytochrome (NrfH), reveals notable, differences in the protein surface around heme 2, which may be the docking, site for the redox partner. The structure shows that four of the NrfA, hemes (hemes 2-5) have bis-histidine axial heme-Fe ligation. The catalytic, heme-Fe (heme 1) has a lysine distal ligand and an oxygen atom proximal, ligand. Analysis of ... [(full description)]
About this StructureAbout this Structure
1GU6 is a [Single protein] structure of sequence from [Escherichia coli] with CA, HEC and GOL as [ligands]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli., Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ, Biochemistry. 2002 Mar 5;41(9):2921-31. PMID:11863430
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