Control of catalysis in flavin-dependent monooxygenases

被引:144
|
作者
Palfey, Bruce A. [1 ]
McDonald, Claudia A. [1 ]
机构
[1] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA
关键词
Flavin; Monooxygenase; Hydroxylase; Hydroperoxide; Peroxide; Oxygen; PARA-HYDROXYBENZOATE HYDROXYLASE; PSEUDOMONAS-FLUORESCENS; CYCLOHEXANONE MONOOXYGENASE; FLAVOPROTEIN MONOOXYGENASES; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURES; PH-DEPENDENCE; HALF-REACTION; WILD-TYPE; MECHANISM;
D O I
10.1016/j.abb.2009.11.028
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:26 / 36
页数:11
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