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

Capa

Citar

Texto integral

Acesso aberto Acesso aberto
Acesso é fechado Acesso está concedido
Acesso é fechado Somente assinantes

Resumo

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.

Texto integral

Acesso é fechado

Sobre autores

Е. Tyunina

G. A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences

Autor responsável pela correspondência
Email: tey@isc-ras.ru
Rússia, Ivanovo, 153045

I. Mezhevoi

G. A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences

Email: tey@isc-ras.ru
Rússia, Ivanovo, 153045

Bibliografia

  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. 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. 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. 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. Li Sh., Hong M. // J. Am. Chem. Soc. 2011. V. 133. P. 1534. https://dx.doi.org/10.1021/ja108943n
  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. Zhang Y. // Annu. Rev. Pharmacol. Toxicol. 2005. V. 45. P. 529. https://doi.org/10.1146/annurev.pharmtox.45.120403.100120
  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. Marinković A.D., Drmanić S.Ž., Jovanović B.Ž. et al. // J. Serb. Chem. Soc. 2005. V. 70. P. 557.
  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. 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. Lugo M.L., Lubes V.R. // J. Chem. Eng. Data. 2007. V. 52. P. 1217. https://doi.org/10.1021/je6005295
  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. 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. Tyunina E.Yu., Mezhevoi I.N. // Ibid. 2023. V. 180. P. 107020. https://doi.org/10.1016/j.jct.2023.107020
  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. 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. 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. 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. 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. Wadsö I., Goldberg R.N. // Pure Appl. Chem. 2001. V. 73. P. 1625.
  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. Archer D.G. // Phys. Chem. Ref. Data. 1999. V. 28. P. 1. https://doi.org/10.1063/1.556034
  24. Баделин В.Г., Смирнов В.И., Межевой И.Н. // Журн. физ. химии. 2002. Т. 76. № 7. С. 1299.
  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. Palecz B. // J. Therm. Anal. Calorim. 1998. V. 54. P. 257.
  27. Palecz B. // J. Am. Chem. Soc. 2005. V. 127. P. 17768.
  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. Chemistry and biochemistry of the amino acids. / Ed. By G.C. Barret, Chapman and Hall, London-N.Y.; 1985.
  30. Pettit L.D. // Pure Appl. Chem. 1984. V. 56. P. 247.
  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. Nagal H., Kuwabara K., Carta G. // J. Chem. Eng. Data. 2008. V. 53. P. 619. https://doi.org/10.1021/je700067a
  33. Ashton L.A., Bullock J. // J. Chem. Soc. Faraday Trans. Part 1. 1982. V. 78. P. 1177.
  34. Ross P.D., Subramanian S. // Biochemistry. 1981. V. 20. P. 3096. https://doi.org/10.1021/bi00514a017
  35. Castronuovo G., Niccoli M., Varriale L. // Tetrahedron. 2007. V. 63. P. 7047. https://doi.org/10.1016/j.tet.2007.05.014
  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. 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. 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. Sabbah R., Ider S. // Can. J. Chem. 1999. V. 77. P. 249. https://doi.org/10.1139/cjc-77-2-249
  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. Haj-Zaroubi M., Schmidtchen F.P. // Chem. Phys. Chem. 2005. V. 6. P. 1181. https://doi.org/10.1002/cphc.200400559

Arquivos suplementares

Arquivos suplementares
Ação
1. JATS XML
2. Fig. 1. Structure of the studied compounds.

Baixar (65KB)
3. Fig. 2. Dependences of enthalpies of transfer of L-histidine (His) from buffer to buffer solution of pyridinecarboxylic acid isomers (1 - INA, 2 - NA, 3 - PA) on PyCOOH concentration at T = 298.15 K. The molality of amino acid mHis=0.0064 mol kg-1.

Baixar (72KB)

Declaração de direitos autorais © Russian Academy of Sciences, 2025