Mechanisms for control of biological electron transfer reactions

被引：18

作者：

Williamson, Heather R. ^{[1
]}

Dow, Brian A. ^{[1
]}

Davidson, Victor L. ^{[1
]}

机构：

[1] Univ Cent Florida, Burnett Sch Biomed Sci, Coll Med, Orlando, FL 32827 USA

来源：

BIOORGANIC CHEMISTRY | 2014年 / 57卷

基金：

美国国家卫生研究院;

关键词：

Amicyanin; Coupled electron transfer; Electronic coupling; Gated electron transfer; Hole hopping; MauG; Quinoprotein; Reorganization energy; AROMATIC AMINE DEHYDROGENASE; SITE-DIRECTED MUTAGENESIS; PYRUVATE FORMATE-LYASE; IONIC-STRENGTH DEPENDENCE; TYPE-1 COPPER SITE; METHYLAMINE DEHYDROGENASE; TRYPTOPHAN TRYPTOPHYLQUINONE; METHANOL DEHYDROGENASE; DNA PHOTOLYASE; PARACOCCUS-DENITRIFICANS;

D O I：

10.1016/j.bioorg.2014.06.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：213 / 221

页数：9

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