The kinetics of electron entry in beef heart cytochrome c oxidase have been studied by stopped-flow spectroscopy following chemical modification of the CuA site with mercurials. In this derivative CuA is no longer reducible by cytochrome c while cytochrome alpha may accept electrons from the latter with rates comparable to the native enzyme. The results indicate that CuA is not the exclusive electron entry site in cytochrome c oxidase.

The kinetics of electron entry in cytochrome c oxidase / Malatesta, F.; Antonin, G.; Sarti, P.; Vallone, B.; Brunori, M.. - In: BIOLOGY OF METALS. - ISSN 0933-5854. - 3:2(1990), pp. 118-121. [10.1007/BF01179517]

The kinetics of electron entry in cytochrome c oxidase

Sarti, P.;Vallone, B.;
1990

Abstract

The kinetics of electron entry in beef heart cytochrome c oxidase have been studied by stopped-flow spectroscopy following chemical modification of the CuA site with mercurials. In this derivative CuA is no longer reducible by cytochrome c while cytochrome alpha may accept electrons from the latter with rates comparable to the native enzyme. The results indicate that CuA is not the exclusive electron entry site in cytochrome c oxidase.
1990
Animals; Binding Sites; Cattle; Copper; Electron Transport; Electron Transport Complex IV; In Vitro Techniques; Kinetics; Myocardium; Oxidation-Reduction
01 Pubblicazione su rivista::01a Articolo in rivista
The kinetics of electron entry in cytochrome c oxidase / Malatesta, F.; Antonin, G.; Sarti, P.; Vallone, B.; Brunori, M.. - In: BIOLOGY OF METALS. - ISSN 0933-5854. - 3:2(1990), pp. 118-121. [10.1007/BF01179517]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1657156
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