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• W2039110541 startingPage "1144" @default.
• W2039110541 abstract "Three bacterial flavoprotein monooxygenases, p-hydroxybenzoate hydroxylase, orcinol hydroxylase, and salicylate hydroxylase, have been examined for steady-state kinetic isotope effects with (4R)-[4-2H]NAD(P)H and (4R)-[4-3H]NAD(P)H. The observed isotope selections are for deuterium, DV = 1.8-3.5 and D(V/K) = 1.7-5.1, and for tritium, T(V/K) = 5-19. For both orcinol hydroxylase and p-hydroxybenzoate hydroxylase, reduction of enzyme-bound FAD by (4R)-[4-2H]NAD(P)H in pre-steady-state assays reveals intrinsic deuterium isotope effects of 10 +/- 2 on this redox step. These values are at the upper end of substrate deuterium effects seen in enzymatic reactions. Suppression of approximately 83% of the intrinsic isotope effects in the overall reaction rate (e.g., kH/kD = 10 down to DV = 2.5) corroborates earlier kinetic data on p-hydroxybenzoate hydroxylase [Husain, M., & Massey. V. (1979) J. Biol. Chem. 254, 6657] and suggests that these bacterial phenolic monooxygenases balance out internal transition states such that no single barrier is fully rate limiting." @default.
• W2039110541 created "2016-06-24" @default.
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• W2039110541 date "1982-03-16" @default.
• W2039110541 modified "2023-09-23" @default.
• W2039110541 title "Kinetic isotope effects in the oxidation of isotopically labeled NAD(P)H by bacterial flavoprotein monooxygenases" @default.
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• W2039110541 doi "https://doi.org/10.1021/bi00535a006" @default.
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