Funk C, Schröder W P, Salih G, Wiklund R, Jansson C
Department of Biochemistry, Stockholm University, Sweden.
FEBS Lett. 1998 Oct 9;436(3):434-8. doi: 10.1016/s0014-5793(98)01179-x.
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.
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。
