|Generate QR code
Open Access
Subscription Access
Bimolecular Recombination of Molecular Oxygen with Sol-Gel Encapsulated Hemoglobin in a Non-Equilibrium Oxygenated T-Conformation
https://doi.org/10.47612/0514-7506-2023-90-2-165-173
Abstract
A method has been developed for sol-gel encapsulation of hemoglobin in the deoxygenated T-conformation followed by saturation of the protein with molecular oxygen (О2). A set-up for sol-gel encapsulation of hemoglobin under anaerobic conditions has been made. Kinetics for the bimolecular recombination of O2 with encapsulated hemoglobin stabilized predominantly in the oxygenated T-conformation (in an ensemble of oxygenated T-conformers) was recorded for the first time by time-resolved absorption spectroscopy. The developed method allows to study in detail the O2-binding properties of non-equilibrium conformational states of hemoglobin, which will make a significant contribution to understanding the mechanism of regulation of O2 binding by both native human hemoglobin and artificial oxygen carriers.
About the Authors
S. V. Lepeshkevich
B. I. Stepanov Institute of Physics of the National Academy of Sciences of Belarus
Belarus
Belarus
Minsk
M. V. Parkhats
B. I. Stepanov Institute of Physics of the National Academy of Sciences of Belarus
Belarus
Belarus
Minsk
B. M. Dzhagarov
B. I. Stepanov Institute of Physics of the National Academy of Sciences of Belarus
Belarus
Belarus
Minsk
References
1. E. Antonini, M. Brunori. Hemoglobin and Myoglobin in their Reactions with Ligands, North-Holland Publication Co., Amsterdam, London (1971)
2. M. F. Perutz. Nature, 228 (1970) 726—739
3. S.-Y. Park, T. Yokoyama, N. Shibayama, Y. Shiro, J. R. H. Tame. J. Mol. Biol., 360 (2006) 690—701
4. S.-I. Adachi, S.-Y. Park, J. R. H. Tame, Y. Shiro, N. Shibayama. Proc. Natl. Acad. Sci. USA, 100, N 12 (2003) 7039—7044
5. N. Shibayama, A. Sato-Tomita, M. Ohki, K. Ichiyanagi, S.-Y. Park. Proc. Natl. Acad. Sci. USA, 117 (2020) 4741—4748
6. J. Baldwin, C. Chothia. J. Mol. Biol., 129 (1979) 175—220
7. F. Schotte, H. S. Cho, J. Soman, M. Wulff, J. S. Olson, P. A. Anfinrud. Chem. Phys., 422 (2013) 98—106
8. Q. H. Gibson. Biochemistry, 38, N 16 (1999) 5191—5199
9. W. A. Eaton, L. K. Hanson, P. J. Stephens, J. C. Sutherland, J. B. R. Dunn. J. Am. Chem. Soc., 100, N 16 (1978) 4991—5003
10. B. I. Greene, R. M. Hochstrasser, R. B. Weisman, W. A. Eaton. Proc. Natl. Acad. Sci. USA, 75, N 11 (1978) 5255—5259
11. J. S. Olson. Mol. Asp. Med., 84 (2022) 101024(1—15)
12. S. V. Lepeshkevich, I. V. Sazanovich, M. V. Parkhats, S. N. Gilevich, B. M. Dzhagarov. Chem. Sci., 12, N 20 (2021) 7033—7047
13. I. Khan, C. F. Shannon, D. Dantsker, A. J. Friedman, J. P.-G. de Apodaca, J. M. Friedman. Biochemistry, 39 (2000) 16099–16109
14. U. Samuni, D. Dantsker, L. J. Juszczak, S. Bettati, L. Ronda, A. Mozzarelli, J. M. Friedman. Biochemistry, 43 (2004) 13674—13682
15. C. Viappiani, S. Bettati, S. Bruno, L. Ronda, S. Abbruzzetti, A. Mozzarelli, W. A. Eaton. Proc. Natl. Acad. Sci. USA, 101, N 40 (2004) 14414—14419
16. C. Viappiani, S. Abbruzzetti, L. Ronda, S. Bettati, E. R. Henry, A. Mozzarelli, W. A. Eaton. Proc. Natl. Acad. Sci. USA, 111, N 35 (2014) 12758—12763
17. T. K. Das, I. Khan, D. L. Rousseau, J. M. Friedman. Biospectroscopy, 5 (1999) S64—S70
18. С. В. Лепешкевич, Н. В. Коновалова, Б. М. Джагаров. Биохимия, 68, № 5 (2003) 676—685 [S. V. Lepeshkevich, N. V. Konovalova, B. M. Dzhagarov. Biochem. Mosc., 68, N 5 (2003) 551—558]
19. Е. Н. Подденежный, А. А. Бойко. Золь-гель синтез оптического кварцевого стекла, УО “ГГТУ им. П. О. Сухого”, Гомель, Беларусь (2002)
20. L. Ronda, S. Bruno, S. Faggiano, S. Bettati, A. Mozzarelli. Method Enzymol., 437 (2008) 311—328
21. S. V. Lepeshkevich, B. M. Dzhagarov. Biochim. Biophys. Acta, 1794 (2009) 103—109
22. S. V. Lepeshkevich, M. V. Parkhats, A. S. Stasheuski, V. V. Britikov, E. S. Jarnikova, S. A. Usanov, B. M. Dzhagarov. J. Phys. Chem. A, 118, N 10 (2014) 1864—1878
23. S. Unzai, R. Eich, N. Shibayama, J. S. Olson, H. Morimoto. J. Biol. Chem., 273, N 36 (1998) 23150—23159
24. S. V. Lepeshkevich, J. Karpiuk, I. V. Sazanovich, B. M. Dzhagarov. Biochemistry, 43, N 6 (2004) 1675—1684
25. S. V. Lepeshkevich, S. A. Biziuk, A. M. Lemeza, B. M. Dzhagarov. Biochim. Biophys. Acta, 1814, N 10 (2011) 1279—1288
26. P. S. Steinbach, R. Ionescu, C. R. Matthews. Biophys. J., 82, N 4 (2002) 2244—2255
27. P. J. Steinbach. J. Chem. Inf. Comp. Sci., 42, N 6 (2002) 1476—1478
28. B. M. Dzhagarov, S. V. Lepeshkevich. Chem. Phys. Lett., 390, N 1-3 (2004) 59—64
29. S. V. Lepeshkevich, N. V. Konovalova, I. I. Stepuro, B. M. Dzhagarov. J. Mol. Struct., 735-736 (2005) 307—313
30. S. V. Lepeshkevich, B. M. Dzhagarov. FEBS J., 272, N 23 (2005) 6109—6119
31. S. V. Lepeshkevich, S. N. Gilevich, M. V. Parkhats, B. M. Dzhagarov. Biochim. Biophys. Acta, 1864, N 9 (2016) 1110—1121
32. S. V. Lepeshkevich, M. V. Parkhats, I. I. Stepuro, B. M. Dzhagarov. Biochim. Biophys. Acta, 1794, N 12 (2009) 1823—1830
Review
For citations:
Lepeshkevich S.V., Parkhats M.V., Dzhagarov B.M. Bimolecular Recombination of Molecular Oxygen with Sol-Gel Encapsulated Hemoglobin in a Non-Equilibrium Oxygenated T-Conformation. Zhurnal Prikladnoii Spektroskopii. 2023;90(2):165-173. (In Russ.) https://doi.org/10.47612/0514-7506-2023-90-2-165-173
Views: 134
Email this article 