Introduction
Enthalpy–entropy compensation is the concept that differences in the standard enthalpy of reaction ΔH0 for different reactions may be compensated for by differences in the standard entropy of reaction ΔS0, and that such compensation is so common as to be almost universal. The concept applies equally to kinetic data, variations in the enthalpy of activation ΔH‡ being compensated for by variations in the entropy of activation ΔS‡. Thermodynamic data are usually obtained from van ’t Hoff plots and activation data from Arrhenius plots. Calorimetric measurements in principle allow enthalpies and entropies to be measured independently and are less susceptible to some of the difficulties discussed here.
Enthalpy–entropy compensation derives ultimately from an observation almost a century ago of a straight-line relation between the logarithm of the frequency factor and...
References
Bushuev MB, Pishchur DP, Nikolaenkovac EB, Krivopalov VP (2016) Compensation effects and relation between the activation energy of spin transition and the hysteresis loop width for an iron(II) complex. Phys Chem Chem Phys 18:16690–16699
Chang Y, Lai JY, Lee DJ (2016) Thermodynamic parameters for adsorption equilibrium of heavy metals and dyes from wastewaters: research updated. Bioresour Technol 222:513–516
Constable F (1925) The mechanism of catalytic decomposition. Proc Roy Soc Lond A 108:355–378
Cooper A, Johnson CM, Lakey JH, Nöllmann M (2001) Heat does not come in different colours: entropy–enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and multiple causes of heat capacity effects in biomolecular interactions. Biophys Chem 93:215–230
Cornish-Bowden A (2002) Enthalpy–entropy compensation: a phantom phenomenon. J Biosci 27:121–126
Cornish-Bowden A (2012) Enthalpy–entropy compensation as deduced from measurements of temperature dependence. In: Gohlke H (ed) Protein-ligand interactions. Wiley-VCH, Weinheim, pp 33–43
Cornish-Bowden A (2017) Enthalpy–entropy compensation and the isokinetic temperature in enzyme catalysis. J Biosci 42:665–670
Dunitz JD (1995) Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem Biol 2:709–712
Exner O (1964) On the enthalpy–entropy relationship. Coll Czech Chem Comm 26:1094–1113
Exner O (1972) Statistics of enthalpy–entropy relationship. 1. Special case. Coll Czech Chem Comm 37:1425–1444
Exner O (1997) How to get wrong results from good experimental data: a survey of incorrect applications of regression. J Phys Org Chem 10:797–813
Hinshelwood CN (1926) On the theory of unimolecular reactions. Proc R Soc Lond Ser A 113:230–233
Ishigami I, Hikita M, Egawa T, Yeh SR, Rousseau DL (2015) Proton translocation in cytochrome c oxidase: insights from proton exchange kinetics and vibrational spectroscopy. Biochim Biophys Acta Bioenerg 1847:98–108
Johnston IA, Goldspink G (1975) Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature. Nature 237:620–622
Krug RR, Hunter WG, Grieger RA (1976a) Enthalpy–entropy compensation. 1. Some fundamental statistical problems associated with analysis of van ’t Hoff and Arrhenius data. J Phys Chem 80:2335–2341
Krug RR, Hunter WG, Grieger RA (1976b) Enthalpy–entropy compensation. 2. Separation of chemical from statistical effect. J Phys Chem 80:2341–2351
Lumry R, Rajender S (1970) Enthalpy–entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers 9:1125–1127
Perez-Benito JF (2013) Some tentative explanations for the enthalpy–entropy compensation effect in chemical kinetics: from experimental errors to the Hinshelwood-like model. Monatsh Chem 144:49–58
Perez-Benito JF, Mulero-Raichs M (2016) Enthalpy–entropy compensation effect in chemical kinetics and experimental errors: a numerical simulation approach. J Phys Chem A 120:7598–7609
Sharp K (2001) Entropy–enthalpy compensation: fact or artifact? Prot Sci 10:661–667
Singh RK, Suzuki T, Mandal T, Balsubramanian N, Haldar M, Mueller DJ, Strode JA, Cook G, Mallik S, Srivastava DK (2014) Thermodynamics of binding of structurally similar ligands to histone deacetylase 8 sheds light on challenges in the rational design of potent and isozyme-selective inhibitors of the enzyme. Biochemistry 53:7445–7458
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Section Editor information
Rights and permissions
Copyright information
© 2018 European Biophysical Societies’ Association (EBSA)
About this entry
Cite this entry
Cornish-Bowden, A. (2018). Entropy-Enthalpy Compensation. In: Roberts, G., Watts, A. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-35943-9_10072-1
Download citation
DOI: https://doi.org/10.1007/978-3-642-35943-9_10072-1
Received:
Accepted:
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-35943-9
Online ISBN: 978-3-642-35943-9
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences