Journal
BIOCHEMISTRY
Volume 40, Issue 11, Pages 3273-3281Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi002167a
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The Cl- channel blocker NPPB (5-nitro-2-(3-phenylpropylamino) benzoic acid) inhibited photosynthetic oxygen evolution of isolated thylakoid membranes in a pH-dependent manner with a K-i of about 2 muM at pH 6. Applying different electron accepters, taking electrons either directly from photosystem II (PS II) or photosystem I (PS I), the site of inhibition was localized within PS IT. Measurements of fluorescence induction kinetics and thermoluminescence suggest that the binding of NPPB to the Q(B) binding site of PS II is similar to the herbicide DCMU (3-(3,4-dichlorophenyl)-1,1-dimethylurea). The effects of different arylaminobenzoate derivatives and other Cl- channel inhibitors on photosynthetic electron transport were investigated. The structure-activity relationship of the inhibitory effect on PS TI shows interesting parallels to the one observed for the arylaminobenzoate block of mammalian Cl- channels. A molecular modeling approach was used to fit NPPB into the Q(B) binding site and to identify possible molecular interactions between NPPB and the amino acid residues of the binding site in PS II. Taken together, these data give a detailed molecular picture of the mechanism of NPPB binding.
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