States with identical steady dissipation rate: Role of kinetic constants in enzyme catalysis

Abstract

A non-equilibrium steady state is characterized by a non-zero steady dissipation rate. Chemical reaction systems under suitable conditions may generate such states. We propose here a method that is able to distinguish states with identical values of the steady dissipation rate. This necessitates a study of the variation of the entropy production rate with the experimentally observable reaction rate in regions close to the steady states. As an exactly-solvable test case, we choose the problem of enzyme catalysis. Link of the total entropy production with the enzyme efficiency is also established, offering a desirable connection with the inherent irreversibility of the process. The chief outcomes are finally noted in a more general reaction network with numerical demonstrations.