PsbO, the manganese-stabilizing protein: Analysis of the structure-function relations that provide insights into its role in photosystem II

被引：58

作者：

Popelkova, Liana ^{[1
]}

Yocum, Charles F. ^{[1
,2
]}

机构：

[1] Univ Michigan, Dept Mol Cellular & Dev Biol, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

来源：

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY | 2011年 / 104卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

Structure-function; Manganese-stabilizing protein; Mutation; Natively unfolded polypeptide; Photosystem II; 33 KDA PROTEIN; OXYGEN-EVOLVING COMPLEX; SITE-DIRECTED MUTAGENESIS; EXTRINSIC 33-KDA PROTEIN; CHLOROPHYLL-CARRYING PROTEIN; WATER-OXIDIZING COMPLEX; AMINO-ACID-SEQUENCES; SP PCC-6803 LACKING; CALCIUM-BINDING; CA2+ BINDING;

D O I：

10.1016/j.jphotobiol.2011.01.015

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：

The minireview presented here summarizes current information on the structure and function of PsbO, the photosystem II (PSI!) manganese-stabilizing protein, with an emphasis on the protein's assembly into PSI!, and its function in facilitating rapid turnovers of the oxygen evolving reaction. Two putative mechanisms for functional assembly of PsbO, which behaves as an intrinsically disordered polypeptide in solution, into PSII are proposed. Finally, a model is presented for the role of PsbO in relation to the function of the Mn, Ca2+, and Cl- cofactors that are required for water oxidation, as well as for the action of hydroxide and small Mn reductants that inhibit the function of the active site of the oxygen-evolving complex. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：179 / 190

页数：12

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