RAS Chemistry & Material ScienceЖурнал физической химии Russian Journal of Physical Chemistry

  • ISSN (Print) 0044-4537
  • ISSN (Online) 3034-5537

Complexation of L-histidine with pyridine carboxylic acid isomers in aqueous buffer solution at 298.15 K: a calorimetric study

PII
S0044453725010081-1
DOI
10.31857/S0044453725010081
Publication type
Article
Status
Published
Authors
Volume/ Edition
Volume 99 / Issue number 1
Pages
89-96
Abstract
The peculiarities of interaction of heterocyclic amino acid of L-histidine (His) with structural isomers of pyridine carboxylic acid: picolinic (PA), nicotinic (NA), and isonicotinic (INA) acids in the phosphate buffer, pH 7.4 at T = 298.15 K, are studied by the method of solution calorimetry. Thermodynamic parameters, viz. binding constants, enthalpies of complexation, Gibbs energies and entropies, are determined. For His and pyridine monocarboxylic acids, the formation of hydrogen bonds and electrostatic interactions is found to be the main force determining the formation of complexes between them in the buffer solution, as evidenced by large negative enthalpy values and positive entropy values. The stability of the obtained complexes depends on the structural isomerism of pyridine carboxylic acid and increases in the series: PA < NA < INA. The main contribution to the stabilization of the formed complexes is shown to be made by the enthalpic component of the Gibbs free energy of complexation.
Keywords
энтальпия растворения гистидин изомеры пиридинмонокарбоновой кислоты буферный раствор термодинамические характеристики
Date of publication
12.09.2025
Year of publication
2025
Number of purchasers
0
Views
7

References

  1. 1. Zhang J., Zhu C., Ma Y. // J. Chem. Thermodynamics. 2017. V. 111. P. 52. http://dx.doi.org/10.1016/j.jct.2017.02.024
  2. 2. Chauhan S., Singh K., Kumar K. et al. // J. Chem. Eng. Data. 2016. V. 61. P. 788. https://doi.org/10.1021/acs.jced.5b00549
  3. 3. Sawhney N., Kumar M., Sharma A.K. et al. // J. Chem. Thermodynamics. 2017. V. 115. P. 156. https://doi.org/10.1016/j.jct.2017.07.040
  4. 4. Tavallali H., Espergham O., Deilamy-Rad G. et al. // Anal. Biochem. 2020. V. 604. P. 113811. https://doi.org/10.1016/j.ab.2020.113811
  5. 5. Li Sh., Hong M. // J. Am. Chem. Soc. 2011. V. 133. P. 1534. https://dx.doi.org/10.1021/ja108943n
  6. 6. Gille A., Bodor E.T., Ahmed K. et al. // Annu. Rev. Pharmacol. Toxicol. 2008. V. 48. P. 79. https://doi.org/10.1146/annurev.pharmtox.48.113006.094746
  7. 7. Zhang Y. // Annu. Rev. Pharmacol. Toxicol. 2005. V. 45. P. 529. https://doi.org/10.1146/annurev.pharmtox.45.120403.100120
  8. 8. El-Dean A.M.K., Abd-Ella A.A., Hassanien R. et al. // ACS Omega. 2019. V. 4. P. 8406. https://doi.org/10.1021/acsomega.9b00932
  9. 9. Marinković A.D., Drmanić S.Ž., Jovanović B.Ž. et al. // J. Serb. Chem. Soc. 2005. V. 70. P. 557.
  10. 10. Gamov G.A., Kiselev A.N., Alexsandriiskii V.V. et al. // J. Mol. Liq. 2017. V. 242. P. 1148. http://dx.doi.org/10.1016/j.molliq.2017.07.106
  11. 11. Al-Saif F.A., Al-Humaidi J.Y., Binjawhar D.N. et al. // J. Mol. Struct. 2020. V. 1218. P. 128547. https://doi.org/10.1016/j.molstruc.2020.128547
  12. 12. Lugo M.L., Lubes V.R. // J. Chem. Eng. Data. 2007. V. 52. P. 1217. https://doi.org/10.1021/je6005295
  13. 13. Tyunina E.Yu., Krutova O.N., Lytkin A.I. // Thermochimica Acta. 2020. V. 690. P. 178704. https://doi.org/10.1016/j.tca.2020.178704
  14. 14. Tyunina E.Yu., Krutova O.N., Lytkin A.I. et al. // J. Chem. Thermodynamics. 2022. V. 171. P. 106809. https://doi.org/10.1016/j.jct.2022.106809
  15. 15. Tyunina E.Yu., Mezhevoi I.N. // Ibid. 2023. V. 180. P. 107020. https://doi.org/10.1016/j.jct.2023.107020
  16. 16. Чернова Р.К., Варыгина О.В., Березкина Н.С. // Изв. Саратовского ун-та. Нов. Сер. Сер. Химия. Биология. Экология. 2015. Т. 15. № 4. С. 15. https://doi.org/10.18500/1816-9775-2015-15-4-15-21
  17. 17. Лыткин А.И., Баделин В.Г., Крутова О.Н. и др. // Журн. общей химии. 2019. Т. 89. № 11. С. 1719. [Lytkin A.I., Badelin V.G., Krutova O.N. et al. // Russ. J. Gen. Chem. 2019. V. 89. P. 2235. https://doi.org/10.1134/S1070363219110124].
  18. 18. Баделин В.Г., Тюнина Е.Ю., Межевой И.Н. // Журн. прикл. химии. 2007. Т. 80. № 5. С. 732. [Badelin V.G., Tyunina E.Yu., Mezhevoi I.N. // Russ. J. Appl. Chem. 2007. V. 80. P. 711.] https://doi.org/10.1134/S1070427207050047
  19. 19. Tyunina E.Yu., Mezhevoi I.N., Dunaeva V.V. // J. Chem. Thermodynamics. 2020. V. 150. P. 106206. https://doi.org/10.1016/j.jct.2020.106206
  20. 20. Smirnov V.I., Badelin V.G. // Thermochim. Acta. 2015. V. 606. P. 41. http://dx.doi.org/10.1016/j.tca.2015.03.007
  21. 21. Wadsö I., Goldberg R.N. // Pure Appl. Chem. 2001. V. 73. P. 1625.
  22. 22. Parker V.B. Thermal properties of univalent electrolytes, vol. 2, Nat. Stand. Ref. Data Ser. Nat. Bur. Stand., US Gov., Washington, DC2, 1965, pp. 66.
  23. 23. Archer D.G. // Phys. Chem. Ref. Data. 1999. V. 28. P. 1. https://doi.org/10.1063/1.556034
  24. 24. Баделин В.Г., Смирнов В.И., Межевой И.Н. // Журн. физ. химии. 2002. Т. 76. № 7. С. 1299.
  25. 25. Tyunina E.Yu., Badelin V.G., Mezhevoi I.N. // J. Mol. Liq. 2019. V. 278. P. 505. https://doi.org/10.1016/j.molliq.2019.01.092
  26. 26. Palecz B. // J. Therm. Anal. Calorim. 1998. V. 54. P. 257.
  27. 27. Palecz B. // J. Am. Chem. Soc. 2005. V. 127. P. 17768.
  28. 28. Бородин В.А., Козловский Е.В., Васильев В.П. // Журн. неорган. химии. 1982. Т. 27. № 9. С. 2169. [Borodin V.A., Kozlovsky E.V., Vasil’ev V.P. // Russ. J. Inorg. Chem. 1982. V. 27. P. 2169–2172].
  29. 29. Chemistry and biochemistry of the amino acids. / Ed. By G.C. Barret, Chapman and Hall, London-N.Y.; 1985.
  30. 30. Pettit L.D. // Pure Appl. Chem. 1984. V. 56. P. 247.
  31. 31. Васильев В.П., Кочергина Л.А., Гаравин В.Ю. // Журн. общ. химии. 1985. Т. 55. С. 2780. [Vasil’ev V.P., Kochergina L.A., Garavin V.Yu. // Russ. J. Gen. Chem. 1985. V. 55. P. 2780.]
  32. 32. Nagal H., Kuwabara K., Carta G. // J. Chem. Eng. Data. 2008. V. 53. P. 619. https://doi.org/10.1021/je700067a
  33. 33. Ashton L.A., Bullock J. // J. Chem. Soc. Faraday Trans. Part 1. 1982. V. 78. P. 1177.
  34. 34. Ross P.D., Subramanian S. // Biochemistry. 1981. V. 20. P. 3096. https://doi.org/10.1021/bi00514a017
  35. 35. Castronuovo G., Niccoli M., Varriale L. // Tetrahedron. 2007. V. 63. P. 7047. https://doi.org/10.1016/j.tet.2007.05.014
  36. 36. Куранова Н.Н. Комплексообразование и кислотно-основные равновесия в водно-органических растворах Cu2+, Fe3+ и никотиновой кислоты: Автореф. дис. … канд. хим. наук. Иваново: ИГХТУ, 2019. 16 с.
  37. 37. Лыткин А.И., Черников В.В., Крутова О.Н. и др. // Журн. физ. химии. 2020. Т. 94. С. 1904. [Lytkin A.I., Chernikov V.V., Krutova O.N., Krutova E.D. // Russ. J. Phys. Chem. A. 2020. V. 94. P. 2569. https://doi.org/10.1134/S003602442012016X]
  38. 38. Лыткин А.И., Черников В.В., Крутова О.Н. и др. // Журн. физ. химии. 2020. Т. 94. № 2. С. 1002. [Lytkin A.I., Chernikov V.V., Krutova O.N., Krutova E.D. // Ibid. A. 2020. V. 94. P. 1342. https://doi.org/10.1134/S0036024420070213]
  39. 39. Sabbah R., Ider S. // Can. J. Chem. 1999. V. 77. P. 249. https://doi.org/10.1139/cjc-77-2-249
  40. 40. Koczoń P., Dobrowolski J.Cz., Lewandowski W. // J. Molec. Struct. 2003. V. 655. P. 89. https://doi.org/10.1016/S0022-2860 (03)00247-3
  41. 41. Haj-Zaroubi M., Schmidtchen F.P. // Chem. Phys. Chem. 2005. V. 6. P. 1181. https://doi.org/10.1002/cphc.200400559
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