2j5m: Difference between revisions
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[[Category: pyrrolidone carboxylic acid]] | [[Category: pyrrolidone carboxylic acid]] | ||
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Revision as of 18:19, 30 October 2007
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STRUCTURE OF CHLOROPEROXIDASE COMPOUND 0
OverviewOverview
We have determined the crystal structure of the chloroperoxidase (CPO), hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution., The intermediate was generated through controlled photoreduction of the, CPO oxygen complex during x-ray data collection, which was monitored by, recording of the crystal absorption spectra. Initially, the peroxo-anion, species was formed and then protonated to yield compound 0. Quantum, chemical calculations indicate that the peroxo-anion species is not stable, and collapses instantaneously to compound 0. Compound 0 is present in the, ferric low-spin doublet ground state and is characterized by a long O O, bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also, observed in the crystal structure.
About this StructureAbout this Structure
2J5M is a [Single protein] structure of sequence from [Leptoxyphium fumago] with NAG, MAN, MN, ACT, HEM, PEO and EDO as [ligands]. Active as [Chloride peroxidase], with EC number [1.11.1.10]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes., Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:17190816
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