Vectorial nature of redox Bohr effects in bovine heart cytochrome c oxidase.
The vectorial nature of redox Bohr effects (redox-linked pK shifts) in cytochrome c oxidase from bovine heart incorporated in liposomes has been analyzed. The Bohr effects linked to oxido-reduction of heme a and CuB display membrane vectorial asymmetry. This provides evidence for involvement of redox Bohr effects in the proton pump of the oxidase.
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Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
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De Nitto
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D000818:Animals; D002248:Carbon Monoxide; D002417:Cattle; D003300:Copper; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000031:analogs & derivatives / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008081:Liposomes; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction
D008081:Liposomes; C027728:heme a; D006418:Heme; D003300:Copper; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV