Doerge D R, Corbett M D
Mol Pharmacol. 1984 Sep;26(2):348-52.
Kinetic and product studies were carried out for the reaction of a synthetic hydroperoxyflavin with a series of organosulfur compounds as a model for the flavin-containing monooxygenase of mammalian liver (FMO). S-Oxidized products were identified, and the kinetics of the oxidation reactions were consistent with a mechanism involving attack of a sulfur nucleophile on the terminal oxygen atom of the hydroperoxyflavin. These results provide information about the substrate oxygenation step of FMO not available from steady-state enzyme kinetics.
以合成的氢过氧黄素与一系列有机硫化合物的反应作为哺乳动物肝脏含黄素单加氧酶（FMO）的模型，进行了动力学和产物研究。鉴定出了S-氧化产物，氧化反应的动力学与涉及硫亲核试剂进攻氢过氧黄素末端氧原子的机制一致。这些结果提供了关于FMO底物氧化步骤的信息，而这些信息无法从稳态酶动力学中获得。
