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. 1989 May 15;260(1):231-5.
doi: 10.1042/bj2600231.

Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides

M Matringe  1 , J M Camadro, P Labbe, R Scalla
Affiliations

Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides

M Matringe et al. Biochem J. .

Abstract

Diphenyl ether herbicides induce an accumulation of protoporphyrin IX in plant tissues. By analogy to human porphyria, the accumulation could be attributed to decreased (Mg or Fe)-chelatase or protoporphyrinogen oxidase activities. Possible effects of acifluorfen-methyl on these enzymes were investigated in isolated corn (maize, Zea mays) etioplasts, potato (Solanum tuberosum) and mouse mitochondria, and yeast mitochondrial membranes. Acifluorfen-methyl was strongly inhibitory to protoporphyrinogen oxidase activities whatever their origins [concn. causing 50% inhibition (IC50) = 4 nM for the corn etioplast enzyme]. By contrast, it was roughly 100,000 times less active on (Mg or Fe)-chelatase activities (IC50 = 80-100 microM). Our results lead us to propose protoporphyrinogen oxidase as a cellular target for diphenyl ether herbicides.

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