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Journal of Bioenergetics and Biomembranes

, Volume 27, Issue 3, pp 263–274 | Cite as

Biological electron transfer

  • Christopher C. Moser
  • Christopher C. Page
  • Ramy Farid
  • P. Leslie Dutton
Article

Abstract

Many oxidoreductases are constructed from (a) local sites of strongly coupled substrate-redox cofactor partners participating in exchange of electron pairs, (b) electron pair/single electron transducing redox centers, and (c) nonadiabatic, long-distance, single-electron tunneling between weakly coupled redox centers. The latter is the subject of an expanding experimental program that seeks to manipulate, test, and apply the parameters of theory. New results from the photosynthetic reaction center protein confirm that the electronic-tunneling medium appears relatively homogeneous, with any variances evident having no impact on function, and that control of intraprotein rates and directional specificity rests on a combination of distance, free energy, and reorganization energy. Interprotein electron transfer between cytochromec and the reaction center and in lactate dehydrogenase, a typical oxidoreductase from yeast, are examined. Rates of interprotein electron transfer appear to follow intraprotein guidelines with the added essential provision of binding forces to bring the cofactors of the reacting proteins into proximity.

Key words

Intra-protein and inter-protein electron transfer oxidoreductases enzyme mechanisms 

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Copyright information

© Plenum Publishing Corporation 1995

Authors and Affiliations

  • Christopher C. Moser
    • 1
  • Christopher C. Page
    • 1
  • Ramy Farid
    • 2
  • P. Leslie Dutton
    • 1
  1. 1.The Johnson Research Foundation and Department of Biochemistry and BiophysicsUniversity of PennsylvaniaPhiladelphia
  2. 2.Department of ChemistryRutgers University at NewarkNewark

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