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Enzyme evolution and entropy production

Physicists are well aware that variational principles are very powerful way of describing the nature. There is no a priori reason why variational principles should not be applied to gain better understanding of biological evolution as well. The minimum entropy production theorem, promoted by Ilya Prigogine, has been the prime candidate for the variational principle from physics relevant for the description of biological phenomena. Recently, Roderick Dewar has derived the maximum entropy production principle, as the general selection principle for nonequilibrium stationary states. In this work we ask the question about present day free energy conversion performed by membrane enzymes important in bioenergetics. When they establish the stationary state is it closer to minimum or to maximum entropy production state? We show that such enzymes operate far from the thermodynamic equilibrium and much closer to the maximum then to the minimum entropy production state. From this result one can assume that biological evolution gradually produced structures designed to keep the system far from equilibrium, when associated dissipation must be high. High dissipation means that the thermodynamic evolution is accelerated in the presence of life. In other words, from the point of view of a physicist, increased entropy is identical goal for the thermodynamic and biological evolution.

enzyme; evolution; entropy production

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