Engineering of N‐terminal threonines in the D1 protein impairs photosystem II energy transfer in Synechocystis 6803

FEBS Letters

Schröder, Wolfgang P¹  Salih, Gaza¹  Funk, Christiane¹  Wiklund, Ronney¹  Jansson, Christer¹ 

[1] Department of Biochemistry, The Arrhenius Laboratories, Stockholm University, S-10691 Stockholm, Sweden

关键词: D1;    Photosystem II;    psbA;    Site-directed mutagenesis;    Synechocystis;    Chl;    chlorophyll;    DCBQ;    2;    6-dichloro-p-benzoquinone;    DCMU;    3-(3;    4-dichlorophenyl)-1;    1-dimethylurea;    HEPES;    N-(2-hydroxyethyl)piperazine-N′-2-ethanesulfonic acid;    QA and QB;    primary and secondary plastoquinone electron acceptors;   

DOI  :  10.1016/S0014-5793(98)01179-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mutants of the cyanobacterium Synechocystis sp. PCC 6803 with N-terminal changes in the photosystem (PSII) II D1 protein were analysed by flash-induced oxygen evolution, chlorophyll a fluorescence decay kinetics and 77 K fluorescence emission spectra. The data presented here show that mutations of the Thr-2, Thr-3 and Thr-4 in D1 do not influence the oxygen evolution. A perturbation on the acceptor side was observed and the importance of the N-terminal threonines for an efficient energy transfer between the phycobilisome and PSII and for stability of the PSII complex was demonstrated.

【 授权许可】

Unknown