engleski

Maximum entropy production as a selection principle for the evolution of enzymatic catalysis

In the biological evolution of enzymatic reaction rates, natural selection has modified various kinetic and structural parameters within the constraints set by the physics of enzymatic catalysis. Here we consider this selection process from a thermodynamic viewpoint. Using a previously calibrated kinetic model of ATP synthesis and hydrolysis, we show that a selection principle of maximum entropy production (MEP) allows accurate prediction of the angular position of the binding transition state of rotary F0F1-ATP synthase in spinach chloroplasts. The same angular position also maximises the Shannon entropy of the enzyme state population distribution. MEP and maximum enzyme state entropy also coincide with the optimal functioning of a general single-cycle Michaelian reaction scheme. Our results support the recent theoretical proposal that MEP is a statistical selection principle underlying a wide range of far-from-equilibrium processes across physics and biology.

entropy production; enzymatic catalysis; optimization

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