Electrochemical methods of evaluating the van't Hoff enthalpy in reactions involving biological macromolecules.
We highlight conditions under which coincidence of van't Hoff and calorimetric enthalpies can be experimentally verified for reactions of biochemical interest. First, we clarify that, often, chemical equations in condensed phase do not explicitly contain information on all processes involved. Second, we underline that the accuracy of electrochemical methods is much higher than that of other non-calorimetric techniques. Electrochemical data on the binding of ethidium ion to DNA are re-examined to verify that the entropy evaluated as the temperature derivative of the free energy agrees in full with the calorimetric one. Third, we point out that unfolding or self-association enthalpies of redox proteins can be reliably obtained by electromotive force measurements, taking advantage of their linkage to redox enthalpies. Thermodynamic cycles coupling biochemical transformations to redox systems are briefly discussed.
Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase, Unità Operativa Università del Molise, Campobasso, Italy.
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D001669:Biochemical Phenomena; D002151:Calorimetry; D003574:Cytochrome c Group / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D004563:Electrochemistry / Q000379:methods*; D004996:Ethidium / Q000737:chemistry; D006418:Heme / Q000737:chemistry; D007202:Indicators and Reagents / Q000737:chemistry; D008962:Models, Theoretical; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D017510:Protein Folding; D013696:Temperature; D013816:Thermodynamics
D003574:Cytochrome c Group; D007202:Indicators and Reagents; D006418:Heme; D004247:DNA; D010088:Oxidoreductases; D004996:Ethidium