Abstract
Specific rates and activation parameters of electron transfer processes were determined for two types of copper-containing proteins which serve as model systems for resolving the role of the polypeptide matrix in these processes. In azurins which are well characterized blue single copper proteins predominantly consisting of a β-sheet polypeptide matrix, the above parameters were determined for the intramolecular long range electron transfer between the pulse radiolytically generated disulphide radical-anions and the copper(II) centre, as a function of driving force and nature of the separating medium in 19 different wild type and single site mutated proteins. The internal ET from the type-1 Cu(I) to the trinuclear Cu(II) centre of ascorbate oxidase is part of this enzyme’s catalytic cycle. We investigated the temperature and pH dependence of this process. Results obtained from studies of both types of proteins correlate with a model based on electron transfer proceeding through well defined pathways using a through-bond tunneling mechanism.
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Farver, O., Pecht, I. (1998). Mechanisms and Control of Electron Transfer Processes in Proteins. In: Canters, G.W., Vijgenboom, E. (eds) Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation. NATO ASI Series, vol 512. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5133-7_5
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DOI: https://doi.org/10.1007/978-94-011-5133-7_5
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