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Proton‐translocating pyrophosphatase of Rhodospirillum rubrum
The membrane of chromatophores of Rhodospirillum rubrum contains an oligomycin-insensitive reversible pyrophosphatase system [l] that is involved in energy transduction by a pathway separate fromExpand
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Proton uptake by cytochrome c oxidase on reduction and on ligand binding.
On reduction, cytochrome oxidase was found to take up 2.4 +/- 0.1 protons in the pH range 7.2-8.5, of which 2 are associated with the binuclear centre, and the remaining fractional proton with haemExpand
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The assignment of the 655 nm spectral band of cytochrome oxidase
The spectral characteristics of the ‘655 nm’ band of cytochrome oxidase were found to be affected by ligands of the binuclear centre, including formate and chloride, and by the resting/pulsedExpand
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[69] Measurement of →H+/O in mitochondria and submitochondrial vesicles
Publisher Summary Quantitative measurement of the translocation of protons through the cristae membrane of mitochondria during the activity of the respiratory chain has assumed increasing importanceExpand
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Rates of cyanide binding to the catalytic intermediates of mammalian cytochrome c oxidase, and the effects of cytochrome c and poly(L-lysine).
Rate constants of cyanide binding to 'fast' oxidase have been measured in the fully-oxidised (O), peroxy (P) and ferryl (F) states at pH 8.0. Values of 2.2, 8 and 10 M-1 s-1, respectively, wereExpand
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Chemiosmotic coupling in cytochrome oxidase
Using the principle of specific vectorial ligand conduction, we outline directly coupled protonmotive O loop and O cycle mechanisms of cytochrome oxidase action that are analogous to protonmotive QExpand
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Protonation states of the catalytic intermediates of cytochrome c oxidase.
Protonation changes accompanying conversion of oxidised (O state) cytochrome c oxidase to the 2-electron-reduced P state, and 3-electron-reduced F state at pH 8.0 have been measured. It was foundExpand
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Binuclear centre structure of terminal protonmotive oxidases
The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re‐examination of existing structural models. A new model is proposed,Expand
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Coupling of charge and proton movement in cytochrome c oxidase
In order to understand the protonmotive chemistry of terminal oxidases, we have explored the question of the degree to which the net charge of the reaction cycle intermediates is counterbalanced byExpand
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