Quantification of flux for non-equilibrium dynamics and thermodynamics for driving non-Michaelis-Menton Enzyme Rates

TL;DR

This paper introduces a novel method to quantify non-equilibrium flux in enzyme dynamics, revealing its role in non-Michaelis-Menton behavior and linking it to thermodynamic quantities like entropy production.

Contribution

It provides the first rigorous quantification of flux driving non-equilibrium enzyme activity and connects it to thermodynamic measures such as chemical potential and entropy production.

Findings

Identified non-equilibrium flux as the cause of non-Michaelis-Menton kinetics.

Quantified the flux, chemical potential, and entropy production in enzyme reactions.

Linked energy input to the thermodynamic driving force of enzyme dynamics.

Abstract

The driving force for active physical and biological systems is determined by both the underlying landscape and the non-equilibrium curl flux. While landscape can be quantified in the experiments by the histograms of the collecting trajectories of the observables, the experimental flux quantification is still challenging. In this work, we studied the single molecule enzyme dynamics and observed the deviation in kinetics from the conventional Michaelis-Menton reaction rate. We identified and quantified the non-equilibrium flux as the origin of such non-Michaelis-Menton enzyme rate behavior. This is the first time of rigorous quantification of the flux for the driving force of the non-equilibrium active dynamics. We also quantified the corresponding non-equilibrium thermodynamics in terms of chemical potential and entropy production. We identified and quantified the origin of the flux, chemical potential and entropy production as the heat absorbed (energy input) in the enzyme reaction.