Electron flow through proteins

被引：117

作者：

Gray, Harry B. ^{[1
]}

Winkler, Jay R. ^{[1
]}

机构：

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

来源：

CHEMICAL PHYSICS LETTERS | 2009年 / 483卷 / 1-3期

关键词：

CYTOCHROME-C-OXIDASE; PSEUDOMONAS-AERUGINOSA AZURINS; BOVINE HEART-MITOCHONDRIA; RESPIRATORY COMPLEX-I; CRYSTAL-STRUCTURE; RIBONUCLEOTIDE REDUCTASE; 2.8-ANGSTROM RESOLUTION; ALKANETHIOL MONOLAYERS; TUNNELING PATHWAYS; TRANSFER KINETICS;

D O I：

10.1016/j.cplett.2009.10.051

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Electron transfers in photosynthesis and respiration commonly occur between metal-containing cofactors that are separated by large molecular distances. Employing laser flash-quench triggering methods, we have shown that 20-angstrom, coupling-limited Fe-II-Ru-III and Cu-I-Ru-III electron tunneling in Ru-modified cytochromes and blue copper proteins can occur on the microsecond timescale both in solutions and crystals. Redox equivalents can be transferred even longer distances by multistep tunneling, often called hopping, through intervening amino acid side chains. Our work has established that 20-angstrom hole hopping through an intervening tryptophan is two orders of magnitude faster than single-step electron tunneling in a Re-modified blue copper protein. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：1 / 9

页数：9

共 72 条

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].