Uncovering enzymatic structural adaptations from energy dissipation

Abstract While genetic mutations, natural selection and environmental pressures are well-known drivers of enzyme evolution, we show that their structural adaptations are significantly influenced by energy dissipation. Enzymes use chemical energy to do work, which results in a loss of free energy due to the irreversible nature of the process. By assuming that the catalytic process occurs along a potential barrier, we describe the kinetics of the conversion of enzyme-substrate complexes to enzyme-product complexes and calculate the energy dissipation. We show that the behaviour of the dissipated energy is a non-monotonic function of the energy of the intermediate state. This finding supports our main result that enzyme configurations evolve to minimise energy dissipation and simultaneously improve kinetic and thermodynamic efficiencies. Our study provides a novel insight into the complex process of enzyme evolution and highlights the crucial role of energy dissipation in shaping structural adaptations.