Control of catalysis in flavin-dependent monooxygenases |
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Authors: | Bruce A. Palfey Claudia A. McDonald |
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Affiliation: | Department of Biological Chemistry, University of Michigan Medical School, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5606, USA |
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Abstract: | Flavoprotein monooxygenases reduce flavins, speed their reaction with oxygen, and stabilize a C4a-oxygen adduct long enough to use this reactive species to transfer an oxygen atom to a substrate. The flavin-oxygen adduct can be the C4a-peroxide anion, in which case it reacts as a nucleophile. The protonated adduct - the C4a-hydroperoxide - reacts as an electrophile. The elimination of H2O2 competes with substrate oxygenation. This side-reaction is suppressed, preventing the waste of NAD(P)H and the production of toxic H2O2. Several strategies have been uncovered that prevent the deleterious side-reaction while still allowing substrate hydroxylation. |
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Keywords: | Flavin Monooxygenase Hydroxylase Hydroperoxide Peroxide Oxygen |
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