Kinetic asymmetry versus dissipation in the evolution of chemical systems as exemplified by single enzyme chemotaxis

TL;DR

This paper investigates the mechanisms behind single enzyme chemotaxis, emphasizing the roles of kinetic and diffusion asymmetries, and argues that systems evolve towards kinetic stability rather than maximum dissipation, with implications for active matter.

Contribution

It demonstrates that kinetic asymmetry and diffusion differences alone determine chemotaxis direction, challenging thermodynamic-centric views and highlighting kinetic stability as a key evolutionary principle.

Findings

Kinetic asymmetry dictates chemotaxis direction.

Diffusion asymmetry influences enzyme movement.

Systems evolve towards kinetic stability, not maximum dissipation.

Abstract

Single enzyme chemotaxis is a phenomenon by which a non-equilibrium spatial distribution of an enzyme is created and maintained by concentration gradients of the substrate and product of the catalyzed reaction. These gradients can arise either naturally through metabolism, or experimentally, e.g., by flow of materials through several channels or by use of diffusion chambers with semipermeable membranes. Numerous hypotheses regarding the mechanism of this phenomenon have been proposed. Here we discuss a mechanism based solely on diffusion and chemical kinetics and show that kinetic asymmetry, a difference in the off rates for substrate and for product, and diffusion asymmetry, a difference in the diffusivities of the bound and free forms of the enzyme, are the sole determinates of the direction of chemotaxis. Exploration of these fundamental symmetries that govern nonequilibrium behavior helps to distinguish between possible mechanisms for the evolution of a chemical system from initial to the steady state, and whether the principle that determines the direction a system shifts when exposed to an external energy source is based on thermodynamics, or on kinetics, with the latter being supported by the results of the present paper. Our results show that while dissipation ineluctably accompanies non-equilibrium phenomena, including chemotaxis, systems do not evolve to maximize dissipation, but rather to attain greatest kinetic stability. Chemotactic response to the gradients formed by other enzymes provides a mechanism for forming loose associations known as metabolons. Significantly the direction of the effective force due to these gradients depends on the kinetic asymmetry of the enzyme, and so can be non-reciprocal, where one enzyme is attracted to another enzyme, but the other enzyme is repelled by the one, an important ingredient in the behavior of active matter.