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Maximum Entropy Production Theorem for Transitions between Enzyme Functional States and Its Applications

1
Mediterranean Institute for Life Sciences, Šetalište Ivana Meštrovića 45, 21000 Split, Croatia
2
Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
3
Faculty of Science, University of Split, Ruđera Boškovića 33, 21000 Split, Croatia
*
Author to whom correspondence should be addressed.
Entropy 2019, 21(8), 743; https://doi.org/10.3390/e21080743
Received: 1 July 2019 / Revised: 26 July 2019 / Accepted: 27 July 2019 / Published: 29 July 2019
(This article belongs to the Special Issue Entropy Production and Its Applications: From Cosmology to Biology)
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Abstract

Transitions between enzyme functional states are often connected to conformational changes involving electron or proton transport and directional movements of a group of atoms. These microscopic fluxes, resulting in entropy production, are driven by non-equilibrium concentrations of substrates and products. Maximal entropy production exists for any chosen transition, but such a maximal transitional entropy production (MTEP) requirement does not ensure an increase of total entropy production, nor an increase in catalytic performance. We examine when total entropy production increases, together with an increase in the performance of an enzyme or bioenergetic system. The applications of the MTEP theorem for transitions between functional states are described for the triosephosphate isomerase, ATP synthase, for β-lactamases, and for the photochemical cycle of bacteriorhodopsin. The rate-limiting steps can be easily identified as those which are the most efficient in dissipating free-energy gradients and in performing catalysis. The last step in the catalytic cycle is usually associated with the highest free-energy dissipation involving proton nanocurents. This recovery rate-limiting step can be optimized for higher efficiency by using corresponding MTEP requirements. We conclude that biological evolution, leading to increased optimal catalytic efficiency, also accelerated the thermodynamic evolution, the synergistic relationship we named the evolution-coupling hypothesis. View Full-Text
Keywords: entropy production; triosephosphate isomerase; ATP synthase; β-lactamases; bacteriorhodopsin entropy production; triosephosphate isomerase; ATP synthase; β-lactamases; bacteriorhodopsin
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Juretić, D.; Simunić, J.; Bonačić Lošić, Ž. Maximum Entropy Production Theorem for Transitions between Enzyme Functional States and Its Applications. Entropy 2019, 21, 743.

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