Abstract
Electron transfer (ET) reactions involving solute biological macromolecules such as metalloproteins, or electron exchanging pigment molecules fixed in transmembrane protein environments possess a number of distinctive features compared with ET reactions between “small” molecules. Some of these features are related to specific properties of the environmental reorganization terms or the inter-reactant work terms which for protein systems include diffusion-like, large amplitude protein conformational motion1−4 and nonlocal or image dielectric forces in both protein and external solvent5,6 A feature of fundamental importance is, however, that biological ET distances frequently exceed the geometric extension of the donor and acceptor groups. While inherent in common diabatic ET theory, this long-range electron tunnel feature raises several questions relating not only to orientation and distance between donor and acceptor groups but also to the relative importance of direct and superexchange ET, and to the effect of environmental configurational fluctuations on the electron tunnel factor.
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Kuznetsov, A.M., Ulstrup, J., Zakaraya, M.G. (1990). Protein Configurational Fluctuation Dependence of the Electronic Tunnel Factor of Modified Metalloprotein Electron Transfer Systems and in Fast Direct and Superexchange Separation and Recombination in Bacterial Photosynthesis. In: Jortner, J., Pullman, B. (eds) Perspectives in Photosynthesis. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 22. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0489-7_19
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DOI: https://doi.org/10.1007/978-94-009-0489-7_19
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