Non-equilibrium variational approach to chemical reactions: application to enzyme kinetics

Abstract

The study of enzyme kinetics is one of the core branches of enzymology. Enzyme reactions are crucial in the study of the origin and preservation of life. Since biological systems function under nonequilibrium conditions, analysing whether a nonequilibrium thermodynamic framework would adequately describe these types of systems is natural. This work presents a theoretical framework based on extended irreversible thermodynamics and variational principles for enzyme kinetics. We show that our model can describe the nonequilibrium region close to the end of the enzymatic reaction, where a transition occurs from non-linear to linear behaviour according to our model. It is argued that this model can describe not only “enzyme-substrate” reactions, but also anywhere we have the action of a catalyst, such as in the study of nanozymes.