Abstract
Halogenated 1,4-benzoquinones are effective inhibitors of photosynthetic electron transport through Photosystem II and the cytochrome b 6 f- complex as well. Due to their properties as vinylogous acid halides they can react with nucleophilic groups of soluble molecules or membrane-bound proteins under formation of a covalent linkage. Despite its high inhibitory properties a 14C-labeled tetrabromo-1,4-benzoquinone (bromanil) shows no Michaelis-Menten type binding behaviour in isolated thylakoids. As detected by its covalent binding, [ 14C]bromanil in isolated spinach cytochrome b 6 f- complex binds to the 20 kDa Rieske iron sulfur protein and the 33–34 kDa cytochrome f. Upon [ 14C]bromanil treatment in spinach thylakoids the highest amount of radioactivity is found in a 20 kDa protein, which may be the Rieske protein, and a 41 kDa protein.
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