Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride
Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride
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DOI:
10.1038/nsmb.1559
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发表时间:
2009-03-01
影响因子:
16.8
通讯作者:
Saenger, Wolfram
中科院分区:
文献类型:
--
作者:
Guskov, Albert;Kern, Jan;Saenger, Wolfram
Photosystem II ( PSII) is a large homodimeric protein-cofactor complex located in the photosynthetic thylakoid membrane that acts as light-driven water: plastoquinone oxidoreductase. The crystal structure of PSII from Thermosynechococcus elongatus at 2.9-angstrom resolution allowed the unambiguous assignment of all 20 protein subunits and complete modeling of all 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer. The presence of a third plastoquinone QC and a second plastoquinone-transfer channel, which were not observed before, suggests mechanisms for plastoquinol-plastoquinone exchange, and we calculated other possible water or dioxygen and proton channels. Putative oxygen positions obtained from a Xenon derivative indicate a role for lipids in oxygen diffusion to the cytoplasmic side of PSII. The chloride position suggests a role in proton-transfer reactions because it is bound through a putative water molecule to the Mn4Ca cluster at a distance of 6.5 angstrom and is close to two possible proton channels. (c) 2009 Nature America, Inc. All rights reserved.