title: Chloroperoxidase, a janus enzyme.
abstract: Chloroperoxidase is a versatile fungal heme-thiolate protein that catalyzes a variety of one-electron and two-electron oxidations. We report here that the alkylation of an essential histidine residue showed no effect on the one-electron peroxidations but inhibited two-electron oxidations. The pH profiles of different peroxidative substrates showed optimal activities at varying pH values for the same enzyme. 2-Allylphenol and substituted ortho-phenolics showed efficient peroxidations. Also, substrates excluded from the active site (or with no favorable positioning at the heme center or heme edge) were converted in the peroxidation reaction. While hydrogen peroxide serves as the superior activator in the two-electron oxidations, small alkylhydroperoxides give much better rates for peroxidation reactions. All the above observations indicate that one-electron oxidations are mechanistically quite different from the two-electron oxidations catalyzed by chloroperoxidase. We propose that the peroxidatic substrates interact predominantly outside the heme active site, presumably at the surface of the enzyme.
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana-Champaign, 6000 South Mathews Avenue, Urbana, Illinois 61801, USA. satyamjayatu@yahoo.com
authors.forename: Kelath Murali
authors.initials: KM
authors.lastname: Manoj
authors.forename: Lowell P
authors.initials: LP
authors.lastname: Hager
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D002711:Chloride Peroxidase / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D005656:Fungal Proteins; D006639:Histidine; D006861:Hydrogen Peroxide; D002711:Chloride Peroxidase