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集胞藻6803中D1蛋白N端苏氨酸的工程改造会损害光系统II的能量传递。

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

作者信息

Funk C, Schröder W P, Salih G, Wiklund R, Jansson C

机构信息

Department of Biochemistry, Stockholm University, Sweden.

出版信息

FEBS Lett. 1998 Oct 9;436(3):434-8. doi: 10.1016/s0014-5793(98)01179-x.

Abstract

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.

摘要

通过闪光诱导的放氧、叶绿素a荧光衰减动力学和77K荧光发射光谱,对集胞藻PCC 6803中光系统(PSII)II D1蛋白N端发生变化的突变体进行了分析。本文给出的数据表明,D1蛋白中苏氨酸-2、苏氨酸-3和苏氨酸-4的突变不影响放氧。观察到受体侧存在扰动,证明了N端苏氨酸对于藻胆体与PSII之间高效能量转移以及PSII复合体稳定性的重要性。

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