Abstract
Using site-directed mutagenesis, it was shown that two histidine residues (his-197 and his-214) in the Photosystem II protein D2 play a crucial role in the function of the Photosystem II complex in the cyanobacterium Synechocystis 6803. A specific change of either histidine residue into tyrosine and asparagine, respectively, lead to a loss of PS II activity. These histidine residues have been hypothesized to be analogous to the histidine residues of the M-subunit from purple bacteria involved in binding of the reaction center chromophore, and Q and Fe , respectively (see ref. 1 and 2). The data presented here can be interpreted to support this hypothesis. The data obtained are consistent with the hypothesis that the binding determinants for the PS II reaction center are created mainly by D1 and D2.
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Vermaas, W.F.J., Williams, J.G.K., Chisholm, D.A., Arntzen, C.J. (1987). Site-Directed Mutagenesis in the Photosystem II Gene psbD, Encoding the D2 Protein. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0519-6_169
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DOI: https://doi.org/10.1007/978-94-017-0519-6_169
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