Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5A resolution

被引：621

作者：

Standfuss, R ^{[1
]}

van Scheltinga, ACT ^{[1
]}

Lamborghini, M ^{[1
]}

Kühlbrandt, W ^{[1
]}

机构：

[1] Max Planck Inst Biophys, Dept Biol Struct, D-60438 Frankfurt, Germany

来源：

EMBO JOURNAL | 2005年 / 24卷 / 05期

关键词：

crystal structure; energy transfer; light harvesting; membrane protein; photosynthesis;

D O I：

10.1038/sj.emboj.7600585

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 plant light-harvesting complex of photosystem II (LHC-II) collects and transmits solar energy for photosynthesis in chloroplast membranes and has essential roles in regulation of photosynthesis and in photoprotection. The 2.5 Angstrom structure of pea LHC-II determined by X-ray crystallography of stacked two-dimensional crystals shows how membranes interact to form chloroplast grana, and reveals the mutual arrangement of 42 chlorophylls a and b, 12 carotenoids and six lipids in the LHC-II trimer. Spectral assignment of individual chlorophylls indicates the flow of energy in the complex and the mechanism of photoprotection in two close chlorophyll a - lutein pairs. We propose a simple mechanism for the xanthophyll-related, slow component of nonphotochemical quenching in LHC-II, by which excess energy is transferred to a zeaxanthin replacing violaxanthin in its binding site, and dissipated as heat. Our structure shows the complex in a quenched state, which may be relevant for the rapid, pH-induced component of nonphotochemical quenching.

引用

页码：919 / 928

页数：10

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