Nonequilibrium chemical potentials and free energies for enzyme-catalyzed reactions.
Using the statistical theory of nonequilibrium thermodynamics we explore the nature of nonequilibrium corrections to chemical potentials in simple enzyme-catalyzed reactions. The statistical definition of the chemical potential, which pertains to systems that are at stable steady states, is applied to the Michaelis-Menten reaction scheme in a cellular-sized compartment that communicates with outside reservoirs. Calculations based on the kinetic parameters for hexokinase and triose phosphate isomerase show that substantial corrections to the chemical potential of product (the order of 25 mV) are possible if the reaction is sufficiently far from equilibrium. The dependence of the corrections to the chemical potentials on the size of the cellular compartment are explored, and the relevance of the corrections for understanding the thermodynamics of metabolites is discussed.
D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004798:Enzymes; D013223:Statistics as Topic; D013816:Thermodynamics
D004798:Enzymes