Ref ID : 4552
Susana Shochat, Noam Adir, Alma Gal, Yorinao Inoue, Laurence Mets, and Itzhak Ohad; Photoinactivation of Photosystem II and Degradation of the D1 Protein are Reduced in a Cytochrome b6/f-Less Mutant of Chlamydomonas reinhardtii. Z.Naturforsch. 45c:395-401, 1990
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The effect of unoccupancy of the Q(B) sithe by plastoquinone of the photoinactivation of reaction center II in a Cyt B6/f-less mutant of Chlamydomonas reinhardtii, B6, was investigated. In these cells the oxidation of plastoquinol generated by electron flow via RC II to plastoquinone and thus the turnover of PQH2/PQ via the Q(B) site are drastically reduced. Reaction center II of the mutant cells was resistant to photoinactivation relative to the control cells as demonstrated by measurements of light-induced destabilization of S2-Q(B)- charge recombination, rise in intrinsic fluorescence and loss of variable fluorescence. These parameters relate to functions involving the reaction center II D1 protein. The light-induced degradation of D1 in the mutant cells was also considerably reduced, with a t(1/2) value of 7 hr as compared, under similar conditions, to about 1.5 hr for the control cells. These results indicate that the photoinactivation of RC II and turnover of the D1 protein are related and require occupancy of the Q(B) site by PQ and its light-driven reduction.