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

FEBS Letters

Ono, Taka-aki¹  Inoue, Yorinao¹  Vass, Imre¹ 

[1] Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

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;   

DOI  :  10.1016/0014-5793(87)81439-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Removal of the 33 kDa extrinsic protein from photosystem (PS) II membranes resulted in markedly increased stabilization of the S₂Q_A ⁻ charge pair as measured by thermoluminescence. The stabilization increase was specific for the S₂Q_A ⁻ 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.

【 授权许可】

Unknown