The extrinsic proteins of Photosystem II

被引：223

作者：

Bricker, Terry M. ^{[1
]}

Roose, Johnna L. ^{[1
]}

Fagerlund, Robert D. ^{[2
]}

Frankel, Laurie K. ^{[1
]}

Eaton-Rye, Julian J. ^{[2
]}

机构：

[1] Louisiana State Univ, Dept Biol Sci, Biochem & Mol Biol Sect, Baton Rouge, LA 70803 USA

[2] Univ Otago, Dept Biochem, Dunedin, New Zealand

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2012年 / 1817卷 / 01期

基金：

美国食品与农业研究所; 美国能源部;

关键词：

PsbO; PsbP; PsbQ; PsbU; PsbV; MANGANESE-STABILIZING PROTEIN; OXYGEN-EVOLVING COMPLEX; SYNECHOCYSTIS SP PCC-6803; 33 KDA PROTEIN; SITE-DIRECTED MUTAGENESIS; PSBP-LIKE PROTEIN; CYANOBACTERIUM THERMOSYNECHOCOCCUS-ELONGATUS; RESOLUTION CRYSTAL-STRUCTURE; SP; PCC; 6803; CYTOCHROME C-550;

D O I：

10.1016/j.bbabio.2011.07.006

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：

In this review we examine the structure and function of the extrinsic proteins of Photosystem II. These proteins include PsbO, present in all oxygenic organisms, the PsbP and PsbQ proteins, which are found in higher plants and eukaryotic algae, and the PsbU, PsbV, CyanoQ and CyanoP proteins, which are found in the cyanobacteria. These proteins serve to optimize oxygen evolution at physiological calcium and chloride concentrations. They also shield the Mn4CaO5 cluster from exogenous reductants. Numerous biochemical, genetic and structural studies have been used to probe the structure and function of these proteins within the photosystem. We will discuss the most recent proposed functional roles for these components, their structures (as deduced from biochemical and X-ray crystallographic studies) and the locations of their proposed binding domains within the Photosystem II complex. This article is part of a Special Issue entitled: Photosystem II. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：121 / 142

页数：22

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