Dynamic Stability and Thermodynamic Characterization in an Enzymatic Reaction at the Single Molecule Level

TL;DR

This paper investigates the thermodynamic and dynamic properties of an enzymatic reaction at the single molecule level, focusing on stability, reaction velocity, and energy efficiency using a multiscale stochastic analysis.

Contribution

It introduces a formalism for multiscale thermodynamic analysis applied to single-molecule enzymatic reactions, revealing how system parameters influence stability and efficiency.

Findings

Stability of enzyme-state distribution depends on system parameters.

Reaction velocity varies with changes in enzyme stability.

Energy conversion efficiency is affected by reaction conditions.

Abstract

In this work we study, at the single molecular level, the thermodynamic and dynamic characteristics of an enzymatic reaction comprising a rate limiting step. We investigate how the stability of the enzyme-state stationary probability distribution, the reaction velocity, and its efficiency of energy conversion depend on the system parameters. We employ in this study a recently introduced formalism for performing a multiscale thermodynamic analysis in continuous-time discrete-state stochastic systems.