Mechanisms for control of biological electron transfer reactions

    Authors

    H. R. Williamson; B. A. Dow;V. L. Davidson

    Comments

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    Abbreviated Journal Title

    Bioorganic Chem.

    Keywords

    Amicyanin; Coupled electron transfer; Electronic coupling; Gated; electron transfer; Hole hopping; MauG; Quinoprotein; Reorganization; energy; AROMATIC AMINE DEHYDROGENASE; SITE-DIRECTED MUTAGENESIS; TRYPTOPHAN; TRYPTOPHYLQUINONE BIOSYNTHESIS; PYRUVATE FORMATE-LYASE; COLI; RIBONUCLEOTIDE REDUCTASE; IONIC-STRENGTH DEPENDENCE; BLUE-COPPER; PROTEINS; METHYLAMINE DEHYDROGENASE; PARACOCCUS-DENITRIFICANS; METHANOL; DEHYDROGENASE; Biochemistry & Molecular Biology; Chemistry, Organic

    Abstract

    Electron transfer (ET) through and between proteins is a fundamental biological process. The rates and mechanisms of these ET reactions are controlled by the proteins in which the redox centers that donate and accept electrons reside. The protein influences the magnitudes of the ET parameters, the electronic coupling and reorganization energy that are associated with the ET reaction. The protein can regulate the rates of the ET reaction by requiring reaction steps to optimize the system for ET, leading to kinetic mechanisms of gated or coupled ET. Amino acid residues in the segment of the protein through which long range ET occurs can also modulate the ET rate by serving as staging points for hopping mechanisms of ET. Specific examples are presented to illustrate these mechanisms by which proteins control rates of ET reactions. (C) 2014 Elsevier Inc. All rights reserved.

    Journal Title

    Bioorganic Chemistry

    Volume

    57

    Publication Date

    1-1-2014

    Document Type

    Article

    Language

    English

    First Page

    213

    Last Page

    221

    WOS Identifier

    WOS:000345698000026

    ISSN

    0045-2068

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