Plant Physiol. Drug Metab Dispos
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Plant Physiology 100:1948-1954 (1992)
© 1992 American Society of Plant Biologists

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Membranes and Bioenergetics

Photosystem II Core Phosphorylation Heterogeneity, Differential Herbicide Binding, and Regulation of Electron Transfer in Photosystem II Preparations from Spinach 1

Maria T. Giardi, Fernanda Rigoni and Roberto Barbato

Institute of Biochemistry and Ecophysiology of Plants-Consiglio Nazionale delle Ricerche, Via Salaria km 29.3, 00016 Monterotondo Scalo, Italy, Department of Biology, Via Trieste 75, 35121 Padova, Italy

The effect of photosystem II core phosphorylation on the secondary quinone acceptor of photosystem II (QB) domain environment was analyzed by comparative herbicide-binding studies with photosystem II preparations from spinach (Spinacia oleracea L.). It was found that phosphorylation reduces the binding affinity for most photosynthetic herbicides. The binding of synthetic quinones and of the electron acceptor 2,6-dichlorophenolindophenol is also reduced by photosystem II phosphorylation. Four photosystem II core populations isolated from membranes showed different extents of phosphorylation as well as different degrees of affinity for photosynthetic herbicides. These findings support the idea that heterogeneity of photosystem II observed in vivo could be, in part, due to phosphorylation.

1 This work was supported by National Council of Research special grant RAISA sub-project 2. This work was presented in part at the International Meeting on Regulation of Chloroplast Biogenesis, August 28, 1991, Crete, Greece.






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Copyright © 1992 by the American Society of Plant Biologists