1vzh: Difference between revisions
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Revision as of 17:15, 30 October 2007
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STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION
OverviewOverview
Some sulfate-reducing and microaerophilic bacteria rely on the enzyme, superoxide reductase (SOR) to eliminate the toxic superoxide anion radical, (O2*-). SOR catalyses the one-electron reduction of O2*- to hydrogen, peroxide at a nonheme ferrous iron center. The structures of, Desulfoarculus baarsii SOR (mutant E47A) alone and in complex with, ferrocyanide were solved to 1.15 and 1.7 A resolution, respectively. The, latter structure, the first ever reported of a complex between, ferrocyanide and a protein, reveals that this organo-metallic compound, entirely plugs the SOR active site, coordinating the active iron through a, bent cyano bridge. The subtle structural differences between the, mixed-valence and the fully reduced SOR-ferrocyanide adducts were, investigated by taking advantage ... [(full description)]
About this StructureAbout this Structure
1VZH is a [Single protein] structure of sequence from [Desulfovibrio baarsii] with FE, CA and FC6 as [ligands]. Active as [Superoxide reductase], with EC number [1.15.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction., Adam V, Royant A, Niviere V, Molina-Heredia FP, Bourgeois D, Structure. 2004 Sep;12(9):1729-40. PMID:15341736
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