Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Henri-Dunant Road, Patumwan, Bangkok 10300, Thailand.
J Biol Chem. 2011 May 13;286(19):16900-9. doi: 10.1074/jbc.M111.222976. Epub 2011 Mar 19.
C4a-hydroperoxyflavin is found commonly in the reactions of flavin-dependent monooxygenases, in which it plays a key role as an intermediate that incorporates an oxygen atom into substrates. Only recently has evidence for its involvement in the reactions of flavoprotein oxidases been reported. Previous studies of pyranose 2-oxidase (P2O), an enzyme catalyzing the oxidation of pyranoses using oxygen as an electron acceptor to generate oxidized sugars and hydrogen peroxide (H(2)O(2)), have shown that C4a-hydroperoxyflavin forms in P2O reactions before it eliminates H(2)O(2) as a product (Sucharitakul, J., Prongjit, M., Haltrich, D., and Chaiyen, P. (2008) Biochemistry 47, 8485-8490). In this report, the solvent kinetic isotope effects (SKIE) on the reaction of reduced P2O with oxygen were investigated using transient kinetics. Our results showed that D(2)O has a negligible effect on the formation of C4a-hydroperoxyflavin. The ensuing step of H(2)O(2) elimination from C4a-hydroperoxyflavin was shown to be modulated by an SKIE of 2.8 ± 0.2, and a proton inventory analysis of this step indicates a linear plot. These data suggest that a single-proton transfer process causes SKIE at the H(2)O(2) elimination step. Double and single mixing stopped-flow experiments performed in H(2)O buffer revealed that reduced flavin specifically labeled with deuterium at the flavin N5 position generated kinetic isotope effects similar to those found with experiments performed with the enzyme pre-equilibrated in D(2)O buffer. This suggests that the proton at the flavin N5 position is responsible for the SKIE and is the proton-in-flight that is transferred during the transition state. The mechanism of H(2)O(2) elimination from C4a-hydroperoxyflavin is consistent with a single proton transfer from the flavin N5 to the peroxide leaving group, possibly via the formation of an intramolecular hydrogen bridge.
C4a-羟过黄素普遍存在于黄素依赖单加氧酶的反应中,在该反应中,它作为一种中间体发挥关键作用,将一个氧原子掺入底物中。直到最近,才报道了其参与黄素蛋白氧化酶反应的证据。先前对吡喃糖 2-氧化酶(P2O)的研究表明,该酶利用氧作为电子受体催化吡喃糖氧化,生成氧化糖和过氧化氢(H2O2),在 P2O 反应中形成 C4a-羟过黄素,然后将 H2O2 作为产物消除(Sucharitakul,J.,Prongjit,M.,Haltrich,D.,和 Chaiyen,P.(2008)生物化学 47,8485-8490)。在本报告中,使用瞬态动力学研究了还原型 P2O 与氧反应的溶剂动力学同位素效应(SKIE)。我们的结果表明,D2O 对 C4a-羟过黄素的形成几乎没有影响。从 C4a-羟过黄素消除 H2O2 的后续步骤被证明受到 SKIE 的调节,其值为 2.8±0.2,并且该步骤的质子库存分析表明呈线性图。这些数据表明,单质子转移过程导致 H2O2 消除步骤的 SKIE。在 H2O 缓冲液中进行的双和单混合停流实验表明,在黄素 N5 位置用氘标记的还原黄素特异性地产生与在 D2O 缓冲液中预平衡的酶进行的实验中发现的类似的动力学同位素效应。这表明黄素 N5 位置的质子负责 SKIE,并且是在过渡态期间转移的飞行质子。从 C4a-羟过黄素中消除 H2O2 的机制与从黄素 N5 向过氧化物离去基团转移单个质子一致,可能通过形成分子内氢键。