Inhibition of Plant Protoporphyrinogen Oxidase by the Herbicide Acifluorfen-Methyl
Debra A. Witkowski, Blaik P. Halling
Abstract
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Debra A. Witkowski, Blaik P. Halling
Abstract
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The effect of acifluorfen-methyl on tetrapyrrole synthesis in greening chloroplasts of Cucumis sativus was examined. Formation of Mg-proto-porphyrin IX from delta-aminolevulinate was reduced 98% by 10 micromolar acifluorfen-methyl. Conversion of protoporphyrin IX to Mg-protoporphyrin IX was unaffected, but protoporphyrin IX synthesis from delta-aminolevulinate was blocked, indicating a site of inhibition prior to the Mg-chelatase. The enzymic oxidation of protoporphyrinogen IX to protoporphyrin IX was highly sensitive to acifluorfen-methyl, indicating that the site of action of the herbicide is the protoporphyrinogen oxidase. ((c) 1989 FMC Corporation. All rights reserved.).
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The effect of acifluorfen-methyl on tetrapyrrole synthesis in greening chloroplasts of Cucumis sativus was examined. Formation of Mg-proto-porphyrin IX from delta-aminolevulinate was reduced 98% by 10 micromolar acifluorfen-methyl. Conversion of protoporphyrin IX to Mg-protoporphyrin IX was unaffected, but protoporphyrin IX synthesis from delta-aminolevulinate was blocked, indicating a site of inhibition prior to the Mg-chelatase. The enzymic oxidation of protoporphyrinogen IX to protoporphyrin IX was highly sensitive to acifluorfen-methyl, indicating that the site of action of the herbicide is the protoporphyrinogen oxidase. ((c) 1989 FMC Corporation. All rights reserved.).
Key concepts: Protoporphyrinogen oxidase, Protoporphyrin IX, Chemistry, Porphyrin, Protoporphyrin, Chloroplast, Tetrapyrrole, Biochemistry