Abstract
When a reaction is accompanied by a change with the speed close to or slower than the reaction rate, a circulating reaction flow can exist among the reaction states in the macroscopic stationary state. If the accompanying change were at equilibrium in the timescale of the relevant reaction, the transition-state theory would hold to eliminate the flow.
Highlights
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The foundation of describing a reaction by rate equations is generally provided from statistical mechanics, but in some textbooks, it is alternatively introduced as transition state theory combined with thermodynamics because understanding the statistical foundation requires knowledge of the master equation and its further development [1], which is not an easy concept for students of biology
The following kinetic rules are derived from this limiting assumption: (1) a reaction can be described with a single set of rate equations; (2) a detailed balance of reaction holds at equilibrium; (3) the circulating flow among reaction states is prohibited; and (4) the affinity of binding is independent of the binding pathways
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The Limitation of the Combination of Transition State Theory and Thermodynamics for the Reactions of Proteins and Nucleic Acids. Received: 23 November 2021 Accepted: 23 December 2021 Published: 25 December 2021
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