Electrogenic proton exchange between cytochrome a active centre and M-aqueous phase. Evidence for cytochrome a -associated input proton wellстатья
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Аннотация:The rate of cyanide binding with the oxidized cytochrome-c oxidase in proteoliposomes is controlled by ionization of a protein group with pK approximately 6.7, the ligand reacting with the protonated enzyme only [(1983) Bioorg. Chem. (USSR) 9, 216-227]. As shown here, the kinetics of cyanide binding depends on the pH inside the proteoliposomes. The reaction rate is affected by the electrical potential difference across the proteoliposome membranes as if the a3-linked ionizable group exchanged H+ with the proteoliposome interior electrogenically. The data corroborate a hypothesis on the existence of a proton well communicating cytochrome oxidase O2-reducing center with the M-aqueous phase.