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- W2032352818 abstract "The metabolism of aldrin and trans-cinnamic acid within the root nodules of soybean (Glycine max. cv. Forrest) was investigated. In vitro studies with microsomal preparations revealed the presence of two distinct monooxygenase enzymes requiring NADPH and molecular oxygen. This was shown by different distributions in membrane fractions from sucrose density gradients. In addition, cinnamic acid hydroxylase was sensitive to carbon monoxide (CO), similar to cytochrome P-450-dependent monooxygenases, whereas aldrin epoxidation was not. Cyanide ion, strongly inhibited the epoxidase, without affecting hydroxylase activity. The superoxide radical (O2−) scavengers, superoxide dismutase and norepinephrine, inhibited aldrin epoxidation but allowed greater cinnamic acid 4-hydroxylase activity. These results indicate aldrin epoxidase, in contrast to cinnamic acid hydroxylase, does not involve cytochrome P-450, and may instead utilize a peroxidase-like hemoprotein." @default.
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- W2032352818 date "1986-08-01" @default.
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- W2032352818 title "Monooxygenases from soybean root nodules: Aldrin epoxidase and cinnamic acid 4-hydroxylase" @default.
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- W2032352818 doi "https://doi.org/10.1016/0048-3575(86)90059-3" @default.
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