title: Reaction of autoxidation products of penicillamine with myeloperoxidase.
abstract: Spectral evidence is presented which shows that penicillamine is able to initiate the formation of the oxidized intermediates of myeloperoxidase in the absence of exogenous hydrogen peroxide. The autoxidation of penicillamine presumably produces superoxide which dismutates spontaneously to form hydrogen peroxide. Thus, the formation of both compounds II and III of myeloperoxidase was observed. We also report that penicillamine can directly reduce cytochrome c and therefore, it could possibly act as a one-electron donor to myeloperoxidase.
authors.affiliation: Department of Chemistry, University of Alberta, Edmonton, Canada.
authors.forename: L A
authors.initials: LA
authors.lastname: Marquez
authors.forename: H B
authors.initials: HB
authors.lastname: Dunford
mesh_terms: D000818:Animals; D002374:Catalase / Q000494:pharmacology; D002417:Cattle; D003574:Cytochrome c Group; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D010396:Penicillamine; D009195:Peroxidase; D013057:Spectrum Analysis; D013154:Spleen / Q000201:enzymology; D013482:Superoxide Dismutase / Q000494:pharmacology; D013481:Superoxides / Q000378:metabolism
chemical_list: D003574:Cytochrome c Group; D013481:Superoxides; D002374:Catalase; D009195:Peroxidase; D013482:Superoxide Dismutase; D010396:Penicillamine