Dunker A M, Lusk J E, Gibbs J H
Biophys Chem. 1980 Feb;11(1):9-16. doi: 10.1016/0301-4622(80)85002-2.
The kinetics of an elementary reaction step are discussed from the viewpoint of the stochastic theory of chemical kinetics. The general form of the rate constant found in the stochastic approach is described and compared with the expression from transition state theory. Whereas the stochastic theory predicts a rate enhancement in cases which are not adiabatic (in the quantum mechanical sense), transition state theory, which is essentially an adiabatic theory of reaction rates, does not permit inclusion of the effect. This effect can be expected to be of greater importance in cases of catalysis by structures, such as enzymes, containing large numbers of vibrational degrees of freedom (particularly low frequency ones) than in cases lacking such structures. The stochastic theory is more general than the transition state theory, the rate constant expression given by the latter being obtainable from the former when restrictive assumptions, including that of adiabaticity, are made. Interpretations of enzyme catalysis based on the transition state theory must thus be viewed as speculative.
从化学动力学的随机理论角度讨论了基元反应步骤的动力学。描述了随机方法中发现的速率常数的一般形式，并与过渡态理论的表达式进行了比较。虽然随机理论预测在非绝热情况（从量子力学意义上讲）下速率会增强，但本质上是反应速率绝热理论的过渡态理论不允许考虑这种效应。可以预期，在由含有大量振动自由度（特别是低频自由度）的结构（如酶）催化的情况下，这种效应比在缺乏此类结构的情况下更为重要。随机理论比过渡态理论更具普遍性，当做出包括绝热性假设在内的限制性假设时，后者给出的速率常数表达式可从前者获得。因此，基于过渡态理论对酶催化的解释必须被视为推测性的。
