Südi J
Abteilung Toxkologie, Christian-Albrechts-Universität, Kiel, Federal Republic of Germany.
Biochem J. 1991 May 15;276 ( Pt 1)(Pt 1):265-8. doi: 10.1042/bj2760265.
A modified way to construct kinetic barrier diagrams is presented. Although the diagram superficially resembles a free-energy profile, it is independent of any conception derived from transition-state theory. Some simple calculations referring to the lactate dehydrogenase turnover reaction at equilibrium demonstrate self-consistency of the diagram and its direct relevance to the results of numerical simulations of the detailed course of enzyme-catalysed reactions.
本文提出了一种构建动力学势垒图的改进方法。尽管该图表面上类似于自由能曲线,但它独立于任何源自过渡态理论的概念。一些关于乳酸脱氢酶在平衡状态下周转反应的简单计算证明了该图的自洽性及其与酶催化反应详细过程数值模拟结果的直接相关性。