Proton coupled electron transfer and redox active tyrosines in Photosystem II

被引:70
作者
Barry, Bridgette A. [1 ,2 ]
机构
[1] Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30332 USA
[2] Georgia Inst Technol, Petit Inst Bioengn & Biosci, Atlanta, GA 30332 USA
基金
美国国家卫生研究院;
关键词
Oxygen evolution; EPR spectroscopy; Manganese cluster; Midpoint potential; Water oxidation; SYNECHOCYSTIS SP PCC-6803; RESONANCE SIGNAL-II; PHOTOSYNTHETIC REACTION-CENTER; MANGANESE-STABILIZING SUBUNIT; SITE-DIRECTED MUTAGENESIS; LINKED STRUCTURAL-CHANGES; HYDROGEN-ATOM TRANSFER; HIGH-FIELD EPR; TYROSYL RADICALS; Y-Z;
D O I
10.1016/j.jphotobiol.2011.01.026
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
In this article, progress in understanding proton coupled electron transfer (PCET) in Photosystem II is reviewed. Changes in acidity/basicity may accompany oxidation/reduction reactions in biological catalysis. Alterations in the proton transfer pathway can then be used to alter the rates of the electron transfer reactions. Studies of the bioenergetic complexes have played a central role in advancing our understanding of PCET. Because oxidation of the tyrosine results in deprotonation of the phenolic oxygen, redox active tyrosines are involved in PCET reactions in several enzymes. This review focuses on PCET involving the redox active tyrosines in Photosystem II. Photosystem II catalyzes the light-driven oxidation of water and reduction of plastoquinone. Photosystem II provides a paradigm for the study of redox active tyrosines, because this photosynthetic reaction center contains two tyrosines with different roles in catalysis. The tyrosines, YZ and YD, exhibit differences in kinetics and midpoint potentials, and these differences may be due to noncovalent interactions with the protein environment. Here, studies of YD and YZ and relevant model compounds are described. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:60 / 71
页数:12
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