Investigation of the effect of MTBE as an environmental pollutant on the structure structure and thermal stability of human carbonic anhydrase II

Document Type : Original Research

Authors

1 Master student in biophysics, Al-Zahra University

2 Assistant Professor of BiophysicsDepartment of Biotechnology, Faculty of Biological Sciences Alzahra University

Abstract
Methyl tertiary-butyl ether (MTBE) One of the gasoline additives used to increase octane and reduce greenhouse gas emissions, MTBE can enter the human blood flow through different ways including inhalation, oral and skin contact. Human carbonic anhydrase is one of the metalloenzymes that is found in almost all living organisms and has been extensively studied and many diseases are associated with carbonic anhydrase. In this study, the effect of MTBE proximity with human carbonic anhydrase II enzyme on enzyme activity was investigated by visible-ultraviolet spectroscopy and changes in enzyme Tm at different concentrations of MTBE were reported. In addition, the structural changes of the enzyme in the presence of MTBE were examined by intrinsic fluorescence spectroscopy. The results show that the enzyme activity in the presence of MTBE is inhibited by liner-complex mechanism. The results of intrinsic fluorescence spectroscopy of the enzyme show changes in the structure of the enzyme in the presence of MTBE. Also, following the binding of MTBE to the enzyme, the thermal stability of the enzyme is reduced and it becomes sensitive to temperature changes.

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Supuran, C. T., & Scozzafava, A. (2000). Carbonic anhydrase inhibitors and their therapeutic potential. Expert Opinion on Therapeutic Patents, 10(5), 575-600.
2. Supuran, C. T. (2010). Carbonic anhydrase inhibitors. Bioorganic & medicinal chemistry letters, 20(12), 3467-3474.
3. Supuran, C. T. (2016). Structure and function of carbonic anhydrases. Biochemical Journal, 473(14), 2023-2032.
4. Huang, K. C., Couttenye, R. A., & Hoag, G. E. (2002). Kinetics of heat-assisted persulfate oxidation of methyl tert-butyl ether (MTBE). Chemosphere, 49(4), 413-420.
5. Hong, J. Y., Wang, Y. Y., Mohr, S. N., Bondoc, F. Y., & Deng, C. (2001). Human cytochrome P450 isozymes in metabolism and health effects of gasoline ethers. Research report (Health Effects Institute), (102), 7-27.
6. Najdegerami, I. H., Maghami, P., Sheikh‐Hasani, V., Hosseinzadeh, G., Sheibani, N., & Moosavi‐Movahedi, A. A. (2017). Antichaperone activity and heme degradation effect of methyl tert‐butyl ether (MTBE) on normal and diabetic hemoglobins. Journal of Molecular Recognition, 30(5), e2596.
7. Davis, J. M., & Farland, W. H. (2001). The paradoxes of MTBE. Toxicological Sciences, 61(2), 211-217.
8. Nyman, P. O. (1961). Purification and properties of carbonic anhydrase from human erythrocytes. Biochimica et biophysica acta, 52(1), 1-12.
9. Walls, D., McGrath, R., & Loughran, S. T. (2011). A Digest of Protein Purification. In Protein Chromatography (pp. 3-23).
10. Innocenti, A., Scozzafava, A., Parkkila, S., Puccetti, L., De Simone, G., & Supuran, C. T. (2008). Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates. Bioorganic & medicinal chemistry letters, 18(7), 2267-2271.
11. Tashian, R. E. (1992). Genetics of the mammalian carbonic anhydrases. Advances in genetics. 1992, Elsevier. p. 321-356., 30, 35.
12. Smith, K. S., & Ferry, J. G. (2000). Prokaryotic carbonic anhydrases. FEMS microbiology reviews, 24(4), 335-366.
13. Khatibi, A., Ma’mani, L., Khodarahmi, R., Shafiee, A., Maghami, P., Ahmad, F., ... & Moosavi-Movahedi, A. A. (2015). Enhancement of thermal reversibility and stability of human carbonic anhydrase II by mesoporous nanoparticles. International journal of biological macromolecules, 75, 67-72.
14. Freskgaard, P. O., Maartensson, L. G., Jonasson, P., Jonsson, B. H., & Carlsson, U. (1994). Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II. Biochemistry, 33(47), 14281-14288.
15. Gharib, R., Khatibi, A., Khodarahmi, R., Haidari, M., & Husseinzadeh, S. (2020). Study of glycation process of human carbonic anhydrase II as well as investigation concerning inhibitory influence of 3-beta-hydroxybutyrate on it. International journal of biological macromolecules, 149, 443-449.
16. Segel ,I.H. (1993). Enzyme kinetics. John Wiley & Sons, New York, Chapter 3-4
17. Supuran, C. T. (2008). Diuretics: from classical carbonic anhydrase inhibitors to novel applications of the sulfonamides. Current pharmaceutical design, 14(7), 641-648.
18. Temperini, C., Cecchi, A., Scozzafava, A., & Supuran, C. T. (2009). Carbonic anhydrase inhibitors. Comparison of chlorthalidone, indapamide, trichloromethiazide, and furosemide X-ray crystal structures in adducts with isozyme II, when several water molecules make the difference. Bioorganic & medicinal chemistry, 17(3), 1214-1221.