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The ATP/ADP-antiporter inhibitors and the substrate ADP suppress the uncoupling effect induced by low (10-20 microM) concentrations of palmitate in mitochondria from skeletal muscle and liver. The inhibitors and ADP are found to (a) inhibit the palmitate-stimulated respiration in the controlled state and (b) increase the membrane potential lowered by(More)
Flash-induced single-electron reduction of cytochrome c oxidase. Compound F (oxoferryl state) by RuII(2,2'-bipyridyl)3(2+) [Nilsson (1992) Proc. Natl. Acad. Sci. USA 89, 6497-6501] gives rise to three phases of membrane potential generation in proteoliposomes with tau values and contributions of ca. 45 microsecond (20%), 1 ms (20%) and 5 ms (60%). The rapid(More)
Zinc ions are shown to be an efficient inhibitor of mitochondrial cytochrome c oxidase activity, both in the solubilized and the liposome reconstituted enzyme. The effect of zinc is biphasic. First there occurs rapid interaction of zinc with the enzyme at a site exposed to the aqueous phase corresponding to the mitochondrial matrix. This interaction is(More)
Generation of DeltaPsi (membrane potential) by cytochrome oxidase proteoliposomes oxidizing superoxide-reduced cytochrome c has been demonstrated. XO+HX (xanthine oxidase and hypoxanthine) were used to produce superoxide. It was found that the generation of DeltaPsi is completely abolished by cyanide (an uncoupler) or by superoxide dismutase, and is(More)
The three-dimensional structure of cytochrome coxidase (COX) reveals two potential input proton channels connecting the redox core of the enzyme with the negatively charged (N-) aqueous phase. These are denoted as the K-channel (for the highly conserved lysine residue, K362 in Rhodobacter sphaeroides COX) and the D-channel (for the highly conserved(More)
Two functional input pathways for protons have been characterized in the heme-copper oxidases: the D-channel and the K-channel. These two proton-conducting channels have different functional roles and have been defined both by X-ray crystallography and by the characterization of site-directed mutants. Whereas the entrance of the D-channel is well-defined as(More)
Addition of high H2O2 concentrations to a peroxy complex of proteoliposome-bound cytochrome oxidase converts the complex to a spectrally distinct species. The difference spectrum of the high-peroxide compound versus the oxidized enzyme is characterized in a visible range by a broad symmetrical band at 580 nm (delta epsilon approximately equal to 4 mM-1(More)
pH changes associated with the mitochondrial cytochrome oxidase reaction with H2O2 have been studied. In the presence of ferricyanide or Tris-phenanthroline complex of CoIII as electron acceptors, reaction of H2O2 with the oxidized cytochrome oxidase is accompanied by a steady proton release with a rate constant of ca. 3 M-1.s-1 at pH 6.8. The acidification(More)
Superoxide dismutase is shown to affect spectral changes observed upon cytochrome c oxidase reaction with H2O2, which indicates a possibility of O2- radicals being formed in the reaction. Using DMPO as a spin trap, generation of superoxide radicals from H2O2 in the presence of cytochrome oxidase is directly demonstrated. The process is inhibited by cyanide(More)
Mitochondrial cytochrome c oxidase is able to oxidize various aromatic compounds like o-dianisidine, benzidine and its derivatives (diaminobenzidine, etc.), p-phenylenediamine, as well as amidopyrine, melatonin, and some other pharmacologically and physiologically active substances via the peroxidase, but not the oxidase mechanism. Although specific(More)