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Nature of biological electron transfer

Nature volume 355, pages 796–802 (1992)Cite this article

Abstract

Powerful first-order analysis of intraprotein electron transfer is developed from electron-transfer measurements both in biological and in chemical systems. A variation of 20 Å in the distance between donors and acceptors in protein changes the electron-transfer rate by 1012-fold. Protein presents a uniform electronic barrier to electron tunnelling and a uniform nuclear characteristic frequency, properties similar to an organic glass. Selection of distance, free energy and reorganization energy are sufficient to define rate and directional specificity of biological electron transfer, meeting physiological requirements in diverse systems.

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Authors and Affiliations

  1. The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania, 19104, USA

    Christopher C. Moser, Jonathan M. Keske, Kurt Warncke, Ramy S. Farid & P. Leslie Dutton

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  1. Christopher C. Moser
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  2. Jonathan M. Keske
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  3. Kurt Warncke
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  4. Ramy S. Farid
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  5. P. Leslie Dutton
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Moser, C., Keske, J., Warncke, K. et al. Nature of biological electron transfer. Nature 355, 796–802 (1992). https://doi.org/10.1038/355796a0

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