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.