Electron hopping through proteins

被引：139

作者：

Warren, Jeffrey J. ^{[1
]}

Ener, Maraia E. ^{[1
]}

Vlcek, Antonin, Jr. ^{[2
,3
]}

Winkler, Jay R. ^{[1
]}

Gray, Harry B. ^{[1
]}

机构：

[1] CALTECH, Beckman Inst, Pasadena, CA 91125 USA

[2] Acad Sci Czech Republ, J Heyrovsky Inst Phys Chem, CZ-18223 Prague, Czech Republic

[3] Queen Mary Univ London, Sch Biol & Chem Sci, London E1 4NS, England

来源：

COORDINATION CHEMISTRY REVIEWS | 2012年 / 256卷 / 21-22期

基金：

美国国家科学基金会;

关键词：

Electron transfer; Multistep tunneling; Hopping maps; Redox proteins azurin; Ribonucleotide reductase; DNA photolyase; MauG; REDUCTASE R2 PROTEIN; RIBONUCLEOTIDE REDUCTASE; DNA PHOTOLYASE; CHLAMYDIA-TRACHOMATIS; MANGANESE(IV)/IRON(III) COFACTOR; CRYSTAL-STRUCTURE; RADICAL INITIATION; DIMER REPAIR; FLOW; MECHANISM;

D O I：

10.1016/j.ccr.2012.03.032

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Biological redox machines require efficient transfer of electrons and holes for function. Reactions involving multiple tunneling steps, termed "hopping," often promote charge separation within and between proteins that is essential for energy storage and conversion. Here we show how semiclassical electron transfer theory can be extended to include hopping reactions: graphical representations (called hopping maps) of the dependence of calculated two-step reaction rate constants on driving force are employed to account for flow in a rhenium-labeled azurin mutant as well as in two structurally characterized redox enzymes, DNA photolyase and MauG. Analysis of the 35 angstrom radical propagation in ribonucleotide reductases using hopping maps shows that all tyrosines and tryptophans on the radical pathway likely are involved in function. We suggest that hopping maps can facilitate the design and construction of artificial photosynthetic systems for the production of fuels and other chemicals. (C) 2012 Elsevier B.V. All rights reserved.

引用

页码：2478 / 2487

页数：10

共 87 条

[1] Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis [J].