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- W2091036227 abstract "Summary The yield of hydroxylation products on oxidation of p-methylanisole with cytochrome P-450 models were examined under various conditions. A system consisting of hemin and thiolester (thioglycolic acid ethylester and cysteine ethylester) induced aromatic intramolecular methyl migration (methyl-NIH shift) during p-hydroxylation, whereas a system containing hemin or Fe(II) ion and thiolcarboxylate (thioglycolic acid and cysteine) did not induce methyl-NIH shift. The order of yields of products with the systems was O-demethylation> o-hydroxylation> m-hydroxylation> methyl-NIH shift⩾ aliphatic hydroxylation. The hemin-thiolester complex is concluded to be a good chemical model of cytochrome P-450-dependent monooxygenases, because it induces a methyl-NIH shift." @default.
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- W2091036227 date "1982-10-01" @default.
- W2091036227 modified "2023-10-14" @default.
- W2091036227 title "Occurrence of aromatic methyl migration (NIH-shift) during oxidation of p-methylanisole by hemin-thiolester complex as a cytochrome P-450 model" @default.
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- W2091036227 doi "https://doi.org/10.1016/s0006-291x(82)80099-5" @default.
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