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Abstract
In tolerant wheat, diclofop metabolism in vivo was rapid (33% in 6 hr) and was sensitive to cytochrome P450 inhibitors (CO, tetcyclasis, and 1-aminobenzotriazole). Microsomal fractions from etiolated wheat seedling shoots were shown to support the in vitro hydroxylation of diclofop in the presence of molecular oxygen and NADPH. Enzyme activity was strongly inhibited by tetcyclasis, but showed less sensitivity to 1-aminobenzotriazole and CO. The major enzymatic reaction product in vitro was isolated and identified by HPLC and electron impact mass spectrometry as the NIH shift product, 2-[4-(2,5-dichloro-4-hydroxyphenoxy)phenoxy]propanoic acid. The enzyme had a pH optimum of 7.4, a V max of 5.7 nmol/mg protein · h, and an apparent K m of 41.6 μ M.
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