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

被引：10

作者：

Funk, C ^{[1
]}

Schröder, WP ^{[1
]}

Salih, G ^{[1
]}

Wiklund, R ^{[1
]}

Jansson, C ^{[1
]}

机构：

[1] Univ Stockholm, Arrhenius Lab, Dept Biochem, S-10691 Stockholm, Sweden

来源：

FEBS LETTERS | 1998年 / 436卷 / 03期

基金：

瑞典研究理事会;

关键词：

D1; photosystem II; psbA; site-directed mutagenesis; Synechocystis;

D O I：

10.1016/S0014-5793(98)01179-X

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：

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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：434 / 438

页数：5

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