Unexpected Electron Transfer in Cryptochrome Identified by Time-Resolved EPR Spectroscopy

被引：44

作者：

Biskup, Till ^{[2
,3
]}

Hitomi, Kenichi ^{[4
,5
]}

Getzoff, Elizabeth D. ^{[4
,5
]}

Krapf, Sebastian ^{[1
]}

Koslowski, Thorsten ^{[1
]}

Schleicher, Erik ^{[1
]}

Weber, Stefan ^{[1
]}

机构：

[1] Univ Freiburg, Inst Phys Chem, D-79104 Freiburg, Germany

[2] Free Univ Berlin, Fachbereich Phys, Berlin, Germany

[3] Univ Oxford, Dept Chem, Oxford OX1 2JD, England

[4] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[5] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 52期

基金：

美国国家卫生研究院;

关键词：

electron transfer; EPR spectroscopy; flavins; radical reactions; tryptophan; DNA PHOTOLYASE; CRYSTAL-STRUCTURE; ARABIDOPSIS-THALIANA; RADICAL TRANSFER; CHARGE-TRANSFER; COMPLEX; PHOTOACTIVATION; MECHANISM; ORIGIN; REPAIR;

D O I：

10.1002/anie.201104321

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Subtle differences in the local sequence and conformation of amino acids can result in diversity and specificity in electron transfer (ET) in proteins, despite structural conservation of the redox partners. For individual ET steps, distance is not necessarily the decisive parameter; orientation and solvent accessibility of the ET partners, and thus the stabilization of the charge-separated states, contribute substantially. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：12647 / 12651

页数：5

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