title: Electron transfer between heme proteins and ceruloplasmin.
abstract: Reduced cytochrome-c, reduced myoglobin and oxyhemoglobin respectively have been oxidized to oxidized cytochrome-c, metmyoglobin and methemoglobin by ceruloplasmin. Metmyoglobin and methemoglobin formation was stoichiometric while oxidized cytochrome-c reacted catalytically. Only 50% methemoglobin was formed which suggested that two hemes out of four could transfer electrons. Hydrogen peroxide was formed in the reaction of reduced cytochrome-c with ceruloplasmin.
authors.affiliation: Dept. of Chemistry, Florida State University, Tallahassee 32306.
authors.forename: J M
authors.initials: JM
authors.lastname: Caffrey
authors.forename: R E
authors.initials: RE
authors.lastname: Shinn
authors.forename: E
authors.initials: E
authors.lastname: Frieden
mesh_terms: D000818:Animals; D002570:Ceruloplasmin; D003574:Cytochrome c Group; D004579:Electron Transport; D006420:Hemeproteins; D008706:Methemoglobin; D008786:Metmyoglobin; D010084:Oxidation-Reduction; D013552:Swine
chemical_list: D003574:Cytochrome c Group; D006420:Hemeproteins; D008786:Metmyoglobin; D008706:Methemoglobin; D002570:Ceruloplasmin