FEBS Letters · 1990 · 37 citations · 16 references
AgricultureBiochemistryPlant BiologyHerbicide Mode Of ActionHerbicide SelectivityPlant BiochemistryHerbicide Structure-activity RelationshipsProtoporphyrinogen Oxidase InhibitionTarget Site InteractionsCompetitive Interaction StrengthHerbicide OxidationHerbicide Oxidative StressHerbicide-crop InteractionsMechanism Of PhytotoxicityProtoporphyrinogen Oxidase Inhibitor Chemistry
The specific binding of the herbicide acifluorfen 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid to corn etioplast membranes is competitively inhibited by protoporphyrinogen IX, the substrate of protoporphyrinogen oxidase. Three other peroxidizing molecules, oxadiazon [5-terbutyl-3-(2,4-dichloro-5-isopropoxyphenyl)-1,3,4-oxadiazol -2-one], LS 82556 [(S)3-N-(methylbenzyl)carbamoyl-5-propionyl-2,6-lutidine], and M&B 39279 [5-amino-4-cyano-1-(2,6-dichloro-4-trifluoromethylphenyl)pyrazol], also compete with acifluorfen for its binding site. The four herbicides thus bind to the same site, or to closely located sites, on the enzyme protoporphyrinogen oxidase.
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Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides
Michel Matringe, Jean‐Michel Camadro, Pierrick Labbé et al. · Biochemical Journal · 1989 · 334 citations · Full text