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Engineering of N‐terminal threonines in the D1 protein impairs photosystem II energy transfer in Synechocystis 6803
Author(s) -
Funk Christiane,
Schröder Wolfgang P,
Salih Gaza,
Wiklund Ronney,
Jansson Christer
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01179-x
Subject(s) - synechocystis , photosystem ii , chemistry , energy transfer , photosystem i , terminal (telecommunication) , photosynthesis , gene transfer , protein engineering , biochemistry , biophysics , biology , gene , enzyme , mutant , computer science , computer network , molecular physics
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.