title: Vectorial nature of redox Bohr effects in bovine heart cytochrome c oxidase.
abstract: 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.
authors.affiliation: Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
authors.forename: N
authors.initials: N
authors.lastname: Capitanio
authors.forename: G
authors.initials: G
authors.lastname: Capitanio
authors.forename: E
authors.initials: E
authors.lastname: De Nitto
authors.forename: S
authors.initials: S
authors.lastname: Papa
mesh_terms: 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
chemical_list: D008081:Liposomes; C027728:heme a; D006418:Heme; D003300:Copper; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV