EFFECTS OF BICARBONATE AND ALPHA-KETOGLUTARATE ON SENSITIVITY OF SACCHAROMYCES CEREVISIAE YEAST TO HYDROGEN PEROXIDE AND IRON IONS

M. M. Bayliak


DOI: http://dx.doi.org/10.30970/sbi.1002.490

Abstract


The effects of sodium bicarbonate on the sensitivity of Saccharomyces cerevisiae yeast to hydrogen peroxide and ferrous sulfate were studied. Viability of yeast cells treated with 10–25 mM H2O2 and 0.1–0.2 mM FeSO4 was significantly decreased when 25 or 50 mM NaHCO3 was added to the medium. In the absence of bicarbonate, the levels of oxidative stress markers, namely protein carbonyls, total and oxidized glutathione in cells exposed to 0.2 mM FeSO4 did not differ from such levels in control cells (without FeSO4). Yeast cells incubated with 0.2 mM FeSO4 and 50 mM NaHCO3 had similar levels of oxidized glutathione and carbonyl groups in proteins but lower level of total glutathione compared to cells treated with FeSO4 in the absence of NaHCO3. Yeast cells exposed to a mixture of “2 mM H2O2 + 2 mM FeSO4” in 50 mM sodium bicarbonate buffer survived better than cells treated with these oxidants in 50 mM potassium phosphate buffer. The addition of 10 mM alpha-ketoglutarate led to the increased yeast survival in both buffers under the treatment with “Fe2+2О2”. The protective effect of alpha-ketoglutarate can be due to its H2O2-scavenging activity. The results suggest that bicarbonate ions can enhance or alleviate the toxic effects of redox-active compounds on S. cerevisiae. Pro/antioxidant effects of bicarbonate ions are likely to depend on the kinetics of interaction between HCO3ˉ and produced ROS.

Keywords: Saccharomyces cerevisiae, alpha-ketoglutarate, bicarbonate ions, carbonate radical, oxidative stress.

Full Text:

PDF

References


1. Andrekopoulos C., Zhang H., Joseph J. et al. Bicarbonate enhances α-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical. Biochemical Journal, 2004; 378: 435-447.
https://doi.org/10.1042/bj20031466
PMid:14640973 PMCid:PMC1223984

2. Arai H., Berlett B.S., Chock, P.B. et al. Effect of bicarbonate on iron-mediated oxidation of low-density lipoprotein. PNAS, 2005; 102(30): 10472-10477.
https://doi.org/10.1073/pnas.0504685102
PMid:16027354 PMCid:PMC1176232

3. Augusto O., Bonini M.G., Amanso A.M. et al. Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology. Free Radical Biology and Medicine, 2002; 32(9): 841-859.
https://doi.org/10.1016/S0891-5849(02)00786-4

4. Bayliak M.M., Lylyk M.P., Vytvytska O.M. et al. Assessment of antioxidant properties of alpha-keto acids in vitro and in vivo. European Food Research and Technology, 2016; 242(2): 179-188.
https://doi.org/10.1007/s00217-015-2529-4

5. Berlett B.S., Chock P.B., Yim M.B. et al. Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide. PNAS, 1990; 87: 389-393.
https://doi.org/10.1073/pnas.87.1.389
PMid:2296594 PMCid:PMC53269

6. Bonini M.G., Fernandes D.C., Augusto O. Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry, 2004; 43: 344-351.
https://doi.org/10.1021/bi035606p
PMid:14717588

7. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 1976; 72: 289-292.
https://doi.org/10.1006/abio.1976.9999
PMid:942051

8. Brooks S.P. A simple computer program with statistical tests for the analysis of enzyme kinetics. BioTechniques, 1992; 72: P. 906-911.

9. Davies M.J. Protein oxidation and peroxidation. Biochemical Journal, 2016; 473(7): 805-825.
https://doi.org/10.1042/BJ20151227
PMid:27026395 PMCid:PMC4819570

10. Elam J.S., Malek K., Rodriguez J.A. et al. An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate. Journal of Biological Chemistry, 2003; 278(23): 21032-21039.
https://doi.org/10.1074/jbc.M300484200
PMid:12649272

11. Jansson P.J., Del Castillo U., Lindqvist C. et al. Effects of iron on vitamin C/copper-induced hydroxyl radical generation in bicarbonate-rich water. Free Radical Research, 2005; 39 (5): 565-570.
https://doi.org/10.1080/10715760400009233
PMid:16036332

12. King D.A., Sheafor M.W., Hurst J.K. Comparative toxicities of putative phagocyte-generated oxidizing radicals toward a bacterium (Escherichia coli) and a yeast (Saccharomyces cerevisiae). Free Radical Biology and Medicine, 2006; 41(5): 765-774.
https://doi.org/10.1016/j.freeradbiomed.2006.05.022
PMid:16895797

13. Levine R.L., Wehr N., Williams J.A. et al. Determination of carbonyl groups in oxidized proteins. Methods in Molecular Biology, 2000; 99: 15-24.
https://doi.org/10.1385/1-59259-054-3:15
PMid:10909073

14. Liochev S.I., Fridovich I. Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions. Proceedings of the National Academy of Sciences (USA), 2004; 101: 12485-12490.
https://doi.org/10.1073/pnas.0404911101
PMid:15310847 PMCid:PMC515086

15. Liochev S.I., Fridovich I. Mechanism of the peroxidase activity of Cu, Zn superoxide dismutase. Free Radical Biology and Medicine, 2010; 48(12): 1565-1569.
https://doi.org/10.1016/j.freeradbiomed.2010.02.036
PMid:20211248

16. Luc R., Vergely C. Forgotten radicals in biology. International Journal of Biomedical Science: IJBS, 2008; 4(4): 255-259.

17. Lushchak O.V., Bayliak M.M., Korobova O.V. et al. Buffer modulation of menadione-induced oxidative stress in Saccharomyces cerevisiae. Redox Reports, 2009; 14: 214-220.
https://doi.org/10.1179/135100009X12525712409454
PMid:19843376 PMCid:PMC3399461

18. Lushchak V., Lushchak L., Mota A. et al. Oxidative stress and antioxidant defences in goldfish Carassius auratus during anoxia and reoxygenation. American Journal of Physiology, 2001; 280: R100-R107.
https://doi.org/10.1152/ajpregu.2001.280.1.R100
PMid:11124139

19. Lushchak V.I. Free radicals, reactive oxygen species, oxidative stress and its classification. Chemico-Biological Interactions, 2014, 224C: 164-175.
https://doi.org/10.1016/j.cbi.2014.10.016
PMid:25452175

20. Medinas D.B., Cerchiaro G., Trindade D.F. et al. The carbonate radical and related oxidants derived from bicarbonate buffer. IUBMB Life, 2007; 59: 255-262.
https://doi.org/10.1080/15216540701230511
PMid:17505962

21. Parker M.D., Boron W.F. The divergence, actions, roles, and relatives of sodium-coupled bicarbonate transporters. Physiological Research, 2013; 93(2): 803-959.
https://doi.org/10.1152/physrev.00023.2012
PMid:23589833 PMCid:PMC3768104

22. Prokopiv T.M., Fedorovych D.V., Boretsky Y.R. et al. Oversynthesis of riboflavin in the yeast Pichia guilliermondii is accompanied by reduced catalase and superoxide dismutases activities. Current Microbiology, 2013; 66(1): 79-87.
https://doi.org/10.1007/s00284-012-0242-0
PMid:23053489

23. Queliconi B.B., Marazzi T.B., Vaz S.M. et al. Bicarbonate modulates oxidative and functional damage in ischemia-reperfusion. Free Radical Biology and Medicine, 2013; 55:46-53.
https://doi.org/10.1016/j.freeradbiomed.2012.11.007
PMid:23195687 PMCid:PMC3995138

24. Stadtman E.R., Levine R.L. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids, 2003; 25(3-4): 207-218.
https://doi.org/10.1007/s00726-003-0011-2
PMid:14661084

25. Toledano M.B., Delaunay-Moisan A., Outten C.E. et al. Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast. Antioxidants and Redox Signaling Journal, 2013; 18(13): 1699-711.
https://doi.org/10.1089/ars.2012.5033
PMid:23198979 PMCid:PMC3771550

26. Vesela A., Milhelm J. The role of carbon dioxide in free radical reactions of the organism. Physiological Research, 2002; 51: 335-339.

27. Yadav A., Mishra P.C. Carbonate radical anion as an efficient reactive oxygen species: Its reaction with guanyl radical and formation of 8-oxoguanine Chemical Physics, 2012; 405: 76-88.
https://doi.org/10.1016/j.chemphys.2012.06.012

28. Zhang H., Joseph J., Gurney M. et al. Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics. Journal of Biological Chemistry, 2002; 277: 1013-1020.
https://doi.org/10.1074/jbc.M108585200
PMid:11682485


Refbacks

  • There are currently no refbacks.


Copyright (c) 2016 Studia biologica