Electron transfer between heme proteins and ceruloplasmin.
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.
Caffrey
J M
JM
Dept. of Chemistry, Florida State University, Tallahassee 32306.
Shinn
R E
RE
Frieden
E
E
D000818:Animals; D002570:Ceruloplasmin; D003574:Cytochrome c Group; D004579:Electron Transport; D006420:Hemeproteins; D008706:Methemoglobin; D008786:Metmyoglobin; D010084:Oxidation-Reduction; D013552:Swine
D003574:Cytochrome c Group; D006420:Hemeproteins; D008786:Metmyoglobin; D008706:Methemoglobin; D002570:Ceruloplasmin