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Removal of 33 kDa extrinsic protein specifically stabilizes the S2QA − charge pair in photosystem II
[摘要]

Removal of the 33 kDa extrinsic protein from photosystem (PS) II membranes resulted in markedly increased stabilization of the S2QA charge pair as measured by thermoluminescence. The stabilization increase was specific for the S2QA charge pair and did not require any special herbicide. The effect was fully reversed by reconstitution with the 33 kDa protein, but not at all by high concentrations of Cl, as opposed to those effects known to be reversed by 200 mM Cl . The data are interpreted as indicating a structural change of the donor and/or acceptor side of PS II dependent on association with the 33 kDa extrinsic protein.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] 33 kDa protein;Photosystem II;S state;Thermoluminescence;Oxygen evolution;Chl;chlorophyll;DCMU;3-(3;4-dichlorophenyl)-1;1'-dimethylurea;Mes;4-morpholineethane-sulfonic acid;PS II;photosystem II;qa and qb;primary and secondary quinone acceptors of PS II [时效性] 
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