Site-Directed Mutagenesis in the Photosystem II Gene psbD, Encoding the D2 Protein View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

Wim F. J. Vermaas , John G. K. Williams , Dexter A. Chisholm , Charles J. Arntzen

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. More... »

PAGES

805-808

Book

TITLE

Progress in Photosynthesis Research

ISBN

978-94-017-0521-9
978-94-017-0519-6

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-017-0519-6_169

DOI

http://dx.doi.org/10.1007/978-94-017-0519-6_169

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002591786


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