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The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton
The crystal structures of cytochrome c oxidase from both bovine and Paracoccus denitrificans reveal two putative proton input channels that connect the heme-copper center, where dioxygen is reduced,Expand
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Transmembrane Charge Separation during the Ferryl-oxo → Oxidized Transition in a Nonpumping Mutant of Cytochrome c Oxidase*
The N139D mutant of cytochrome c oxidase from Rhodobacter sphaeroides retains full steady state oxidase activity but completely lacks proton translocation coupled to turnover in reconstitutedExpand
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Cytochrome c, an ideal antioxidant.
Generation of DeltaPsi (membrane potential) by cytochrome oxidase proteoliposomes oxidizing superoxide-reduced cytochrome c has been demonstrated. XO+HX (xanthine oxidase and hypoxanthine) were usedExpand
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Time-resolved single-turnover of ba3 oxidase from Thermus thermophilus.
The kinetics of the oxidation of fully-reduced ba(3) cytochrome c oxidase from Thermus thermophilus by oxygen were followed by time-resolved optical spectroscopy and electrometry. Four catalyticExpand
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Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc 1 site of the mitochondrial respiratory chain
Antimycin, 2‐nonyl‐4‐hydroxyquinoline N‐oxide and funiculosin induce O·− 2 generation by submitochondrial particles oxidizing succinate, whereas KCN, mucidin, myxothiazol or 2,3‐dimercaptopropanolExpand
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Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction-centre complex from Rhodopseudomonas viridis.
Electrogenic and redox events in the reaction-centre complexes from Rhodopseudomonas viridis have been studied. In contrast to the previous points of view it is shown that all the four hemes of theExpand
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Flash‐induced membrane potential generation by cytochrome c oxidase
Flash‐induced single‐electron reduction of cytochrome c oxidase. Compound F (oxoferryl state) by RuII(2,2'‐bipyridyl)2+ 3 [Nilsson (1992) Proc. Natl. Acad. Sci. USA 89, 6497‐6501] gives rise to threeExpand
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Involvement of intramitochondrial protons in redox reactions of cytochrome a
The energy-conserving function of mitochondrial cytochrome oxidase has been widely believed to consist in the transmembrane transfer of an electron [l-4], as originally proposed by Mitchell [5]. OnExpand
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Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochrome c oxidase.
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. TheseExpand
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H2O2‐Induced Conversion of Cytochrome c Oxidase Peroxy Complex to Oxoferryl State
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-peroxideExpand
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