论文标题
了解双氧结合和激活对HOD酶的自旋交叉动力学效应
Understanding the Spin Crossover Dynamical Effects of the Dioxygen Binding and Activation on HOD enzyme
论文作者
论文摘要
对于无辅助因子1-H-3-羟基-4-氧quinaldine-2,4-二氧酶（HOD），二氧化基因（O2）依赖性步骤是速率限制的，并且旋转状态交叉对单线旋转状态。在这里，研究了2-甲基-3-羟基-4（1H） - 奎尼酮（MHQ）上的主要三重型O2分子激活，并通过直接比较BORN-OPPHENHEEIMER DYNAGITS和非亚糖型表面希望型动力学的结果直接比较结果，从而突出了间隔系统交叉效应的催化作用。这项工作证实非绝热动力学效应对于调节基板MHQ的O2激活至关重要。从三重态到单线状态的平衡和转换的时间尺度应在数百个飞秒的范围内。我们希望这项工作能为我们提供有关涉及多个旋转状态的二氧化激活反应的潜在物理。
For the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine-2,4-dioxygenase (HOD), the dioxygen (O2) dependent steps are rate-limiting along with a spin state crossover to the singlet spin state. Here, the primary triplet O2 molecule activation on the 2-methyl-3-hydroxy-4(1H)-quinolone (MHQ) is investigated, and the catalytic role of the intersystem crossing effects is highlighted by directly comparing results from the Born-Oppenheimer dynamics and non-adiabatic surface hopping dynamics. This work confirms non-adiabatic dynamical effects are essential to modulate the O2 activation on the substrate MHQ. The time scale of the equilibration and conversion from triplet to singlet state should be in the range of a few hundreds of femtoseconds. We hope this work provides us a fresh look at the underlying physics of dioxygen activation reactions involving more than one spin state.
