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| - Rate Constants in Two Dimensions of Electron Transfer between Pyruvate Oxidase,a Membrane Enzyme, and Ubiquinone (Coenzyme Q8), Its Water-Insoluble ElectronCarrier
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| - The functionality of the membrane-bound, ubiquinone-dependent pyruvate oxidase from therespiratory chain of Escherichiacoli was reconstituted with a supported lipidic structure. The artificialstructure was especially designed to allow the electrochemical control of the quinone pool through thelateral mobility of the ubiquinone (Q8) molecules. The kinetic coupling of the enzyme bound to the lipidstructure with the quinone pool was ensured by the regeneration of the oxidized form of ubiquinone atthe electrochemical interface. Such an experimental approach enabled us to carry out an unprecedenteddetermination of the kinetic parameters controlling the reaction between the enzyme bound and the electroncarrier under conditions taking rigorously into account the fact that the freedom of motion is restricted totwo dimensions. The kinetic constants we found show that the activated enzyme can be efficiently regulatedby the oxidation level of the quinone pool in natural membranes.
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