Structural highlights
FunctionPRXC_LEPFU Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||||||
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