Abstract
Calorimetry is used to measure the heats of interaction between an L-glutathione solution and HNO3 solutions at a temperature of 298.15 K and ionic strengths of 0.5, 1.0, and 1.5 М (KNO3 background electrolyte). Literature data on the stepwise dissociation constants of L-glutathione are extrapolated to zero ionic strength. Values \({\text{p}}K_{1}^{0}\) = 2.05 ± 0.03, \({\text{p}}K_{2}^{0}\) = 3.49 ± 0.03, \({\text{p}}K_{3}^{0}\) = 8.65 ± 0.05, and \({\text{p}}K_{4}^{0}\) = 9.60 ± 0.05 are obtained and the stepwise peptide ionization constants at fixed ionic strength values are calculated (I = 0.5, 1.0, 1.5 М). The values of the heat of dissociation of the tripeptide are calculated using the universal HEAT program. Standard thermodynamic characteristics (ΔrH°, ΔrG°, and ΔrS°) of reactions of acid–base interaction in L-glutathione aqueous solutions are calculated. The effect the concentration of the background electrolyte has on the enthalpy of peptide dissociation is considered.
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This work was supported by the Russian Foundation for Basic Research, and by the Government of Ivanovo oblast as part of science project no. 18-43-370018.
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Translated by Z. Smirnova
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Lytkin, A.I., Krutova, O.N., Tyunina, E.Y. et al. Thermochemical Study of Reactions of Acid–Base Interaction in an L-Glutathione Aqueous Solution. Russ. J. Phys. Chem. 95, 2051–2054 (2021). https://doi.org/10.1134/S0036024421100162
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DOI: https://doi.org/10.1134/S0036024421100162