Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Nat Chem. 2012 Jan 29;4(3):161-8. doi: 10.1038/nchem.1223.
Fast motions (femtosecond to picosecond) and their potential involvement during enzyme-catalysed reactions have ignited considerable interest in recent years. Their influence on reaction chemistry has been inferred indirectly from studies of the anomalous temperature dependence of kinetic isotope effects and computational simulations. But can such motion reduce the width and height of energy barriers along the reaction coordinate, and contribute to quantum mechanical and/or classical nuclear-transfer chemistry? Here we discuss contemporary ideas for enzymatic reactions invoking a role for fast 'promoting' (or 'compressive') motions that, in principle, can aid hydrogen-transfer reactions. Of key importance is the direct demonstration of a role for compressive motions and the ability to understand in atomic detail the structural origin of these fast motions, but so far this has not been achieved. Here we discuss both indirect experimental evidence that supports a role for compressive motion and the additional insight gained from computational simulations.
近年来，快速运动（飞秒到皮秒）及其在酶催化反应中的潜在作用引起了相当大的兴趣。它们对反应化学的影响是通过研究动力学同位素效应的异常温度依赖性和计算模拟间接推断出来的。但是，这种运动是否可以降低反应坐标上能量势垒的宽度和高度，并有助于量子力学和/或经典核转移化学呢？在这里，我们讨论了当前关于酶促反应的观点，即需要快速的“促进”（或“压缩”）运动来辅助氢转移反应。关键是要直接证明压缩运动的作用，并能够从原子细节上理解这些快速运动的结构起源，但到目前为止，这一点尚未实现。在这里，我们讨论了支持压缩运动作用的间接实验证据，以及从计算模拟中获得的额外见解。
