Next Article in Journal
Deep Reinforcement Learning-Based Traffic Signal Control Using High-Resolution Event-Based Data
Next Article in Special Issue
Entropy Production and Its Application to the Coupled Nonequilibrium Processes of ATP Synthesis
Previous Article in Journal
Entropy? Exercices de Style
Previous Article in Special Issue
Time–Energy and Time–Entropy Uncertainty Relations in Nonequilibrium Quantum Thermodynamics under Steepest-Entropy-Ascent Nonlinear Master Equations
Open AccessReview

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

Mediterranean Institute for Life Sciences, Šetalište Ivana Meštrovića 45, 21000 Split, Croatia
Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
Faculty of Science, University of Split, Ruđera Boškovića 33, 21000 Split, Croatia
Author to whom correspondence should be addressed.
Entropy 2019, 21(8), 743;
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)
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
Show Figures

Figure 1

MDPI and ACS Style

Juretić, D.; Simunić, J.; Bonačić Lošić, Ž. Maximum Entropy Production Theorem for Transitions between Enzyme Functional States and Its Applications. Entropy 2019, 21, 743.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Search more from Scilit
Back to TopTop