Effect of Peroxynitrite and  tert -Butyl Hydroperoxide on Thiol Ligands of Dinitrosyl Iron Complexes

I. S. Pugachenko; Пугаченко И. С.; E. I. Nasybullina; Насыбуллина Э. И.; O. V. Kosmachevskaya; Космачевская О. В.; K. B. Shumaev; Шумаев К. Б.; A. F. Topunov; Топунов А. Ф.

doi:10.31857/S0555109923050148

Effect of Peroxynitrite and tert-Butyl Hydroperoxide on Thiol Ligands of Dinitrosyl Iron Complexes

Authors: Pugachenko I.S.¹, Nasybullina E.I.¹, Kosmachevskaya O.V.¹, Shumaev K.B.¹, Topunov A.F.¹
Affiliations:
1. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences
Issue: Vol 59, No 5 (2023)
Pages: 440-449
Section: Articles
URL: https://journal-vniispk.ru/0555-1099/article/view/138810
DOI: https://doi.org/10.31857/S0555109923050148
EDN: https://elibrary.ru/NSHBED
ID: 138810

Cite item

Full Text

Open Access
Restricted Access

Access granted
Restricted Access

Subscription Access

Abstract
About the authors
References
Supplementary files
Statistics

Abstract

Low molecular weight dinitrosyl iron complexes (DNICs) with thiol-containing ligands are a physiological form for deposit and transport of nitric oxide (NO) in the organism, herewith DNICs can exhibit antioxidant and antiradical properties. It was that DNICs containing cysteine, glutathione and lipoic acid as ligands, decreased the rate of dihydrodamine oxidation by peroxynitrite formed during 3-morpholinononymine decomposition. Thiol (sulfhydryl) ligands are present in DNICs in the form of thiolate anions (R-S⁻), which protects these groups from oxidation by peroxynitrite. When tert-butyl peroxide was used as an oxidizer at low concentration, the protective effect of DNICs on their SH-groups was observed for complexes with lipoic acid (LA-DNIC) and with glutathione (GS-DNIC). LA-DNIC was more resistant to oxidizing agents and more effective peroxynitrite trap than other DNICs. DNICs associated with bovine serum albumin had a negligible protective effect on cysteine residue during oxidation by peroxynitrite and tert-butyl hydroperoxide. The obtained results allow us to consider low molecular weight DNICs with thiol ligands as peroxynitrite traps and thiol residues protectors in proteins.

Keywords

dinitrosyl iron complexes, thiols, tert-butyl hydroperoxide, peroxynitrite

References

Hsiao H.-Y., Chung C.-W., Santos J.H., Villaflores O.B., Lu T.-T. // Dalton Transactions. 2019. V. 48. № 26. P. 9431–9453.
Vanin A.F. // Nitric Oxide. 2016. V. 54. P. 15–29.
Vanin A.F., Mokh V.P., Serezhenkov V.A., Chazov E.I. // Nitric Oxide. 2007. V. 16. № 3. P. 322–330.
Kapelko V.I., Lakomkin V.L., Abramov A.A., Lukoshkova E.V., Undrovinas N.A., Khapchaev A.Y., Shirinsky V.P. // Oxid. Med. Cell. Longev. 2017. V. 2017. e9456163. https://doi.org/10.1155/2017/9456163
Remizova M.I., Kochetygov N.I., Gerbout K.A., Lakomkin V.L., Timoshin A.A., Burgova E.N., Vanin A.F. // Eur. J. Pharmacol. 2011. V. 662. № 1–3. P. 40–46.
Bor-Kucukatay M., Wenby R.B., Meiselman H.J., Baskurt O.K. // Am. J. Physiol. Heart Circ. Physiol. 2003. V. 284. P. 1577–1584.
Shamova E.V., Bichan O.D., Drozd E.S., Gorudko I.V., Chizhik S.A., Shumaev K.B. et al. // Biophysics. 2011. V. 56. № 2. P. 237–242.
Igrunkova A., Fayzullin A., Serejnikova N., Lipina T., Pekshev A., Vanin A. et al. // Int. J. Mol. Sci. 2023. V. 24. № 5. e4439. https://doi.org/10.3390/ijms24054439
Чазов Е.И., Родненков О.В., Зорин А.В., Лакомкин В.Л., Грамович В.В., Выборов О.Н. и др. // Кардиология. 2011. Т. 51. № 11. С. 28–37.
Родненков О.В., Зорин А.В., Гостеев А.Ю., Драгнев А.Г., Чазов Е.И. // Евразийский Кардиологический Журнал. 2016. № 3. С. 186–187.
Shumaev K.B., Petrova N.E., Zabbarova I.V., Vanin A.F., Topunov A.F., Lankin V.Z., Ruuge E.K. // Biochemistry (Moscow). 2004. V. 69. № 5. P. 569–574.
Shumaev K.B., Gubkin A.A., Serezhenkov V.A., Lobysheva I.I., Kosmachevskaya O.V., Ruuge E.K. et al. // Nitric Oxide. 2008. V. 18. № 1. P. 37–46.
Shumaev K.B., Kosmachevskaya O.V., Grachev D.I., Timoshin A.A., Topunov A.F., Lankin V.Z., Ruuge E.K. // Biochemistry (Moscow), Supplement Series B: Biomedical Chemistry. 2021. V. 15. № 4. P. 313–319.
Kosmachevskaya O.V., Nasybullina E.I., Shumaev K.B., Chumikina L.V., Arabova L.I., Yaglova N.V. et al. // Appl. Biochem. Microbiol. 2021. V. 57. № 4. P. 411–420.
Kosmachevskaya O.V., Nasybullina E.I., Shumaev K.B., Novikova N.N., Topunov A.F. // Int. J. Mol. Sci. 2021. V. 22. № 24. e13649. https://doi.org/10.3390/ijms222413649
Martusevich A.K., Soloveva A.G., Dmitrochenkov A.V., Ezhevskaya A.A., Razumovsky A.V. // Annual Research & Review in Biology. 2018. V. 26. № 6. P. 1–11.
Martusevich A.K., Soloveva A.G., Peretyagin S.P., Davyduk A.V. // Biophysics. 2014. V. 59. № 6. P. 954–959.
Dungel P., Perlinge M., Weidinger A., Redl H., Kozlov A.V. // Free Radic. Biol. Med. 2015. V. 89. P. 300–310.
Shumaev K.B., Dudylina A.L., Ivanova M.V., Pugachenko I.S., Ruuge E.K. // BioFactors. 2018. V. 44. № 3. P. 237–244.
Shumaev K.B., Gorudko I.V., Kosmachevskaya O.V., Grigoryeva D.V., Panasenko O.M., Vanin A.F., Topunov A.F. et al. // Oxid. Med. Cell. Longev. 2019. V. 2019. e2798154. https://doi.org/10.1155/2019/2798154
Vanin A.F., Pekshev A.V., Vagapov A.B., Sharapov N.A., Lakomkin V.L., Abramov A.A. et al. // Biophysics (Oxf). 2021. V. 66. № 1. P. 155–163.
Vanin A.F., Tronov V.A., Borodulin R.R. // Cell Biochem. Biophys. 2021. V. 79. № 1. P. 93–102.
Vanin A.F. // Biochemistry (Moscow). 2022. V. 87. № 11. P. 1367–1386.
Bosworth C.A., Toledo J.C. Jr., Zmijewski J.W., Lancaster J.R. // Proc. Natl. Acad. Sci. USA. 2009. V. 106. № 12. P. 4671–4676.
Karoui H., Hogg N., Kalyanaraman B. // Arch. Biochem. Biophys. 1996. V. 330. № 1. P. 115–124.
Shumaev K.B., Kosmachevskaya O.V., Timoshin A.A., Vanin A.F., Topunov A.F. // Methods Enzymol. 2008. V. 436. P. 445–461.
Singh R.J., Hogg N., Joseph J., Konorev E., Kalyanaraman B. // Arch. Biochem. Biophys. 1999. V. 361. № 2. P. 331–339.
Hoff S., Larsen F.H, Andersen M.L., Lund M.N. // Analyst. 2013. V. 138. № 7. P. 2096–2103.
Laemmli U.K. // Nature. 1970. V. 227. № 5259. P. 680–685.
Vanin A.F., Poltorakov A.P., Mikoyan V.D., Kubrina L.K., Burbaev D.S. // Nitric Oxide. 2011. V. 23. № 2. P. 136–149.
Flinck M., Kramer S.H., Pedersen S.F. // Acta Physiol. (Oxf). 2018. V. 223. № 3. e13068. https://doi.org/10.1111/apha.13068
Лобышева И.И., Сереженков В.А., Ванин А.Ф. // Биохимия. 1999. V. 64. № 2. P. 194–200.
Tien M., Bucher J.R., Aust S.D. // Biochem. Biophys. Res. Commun. 1982. V. 107. № 1. P. 279–285.
Younes M., Strubelt O. // J. Appl. Toxicol. 1990. V. 10. № 5. P. 319–324.
Olson A.S., Jameson A.J., Kyasa S.K., Evans B.W., Dussault P.H. // ACS Omega. 2018. V. 3. № 10. P. 14054–14063.
Daiber A., Daub S., Bachschmid M., Schildknecht S., Oelze M., Steven S. et al. // Int. J. Mol. Sci. 2013. V. 14. № 4. P. 7542–7570.
Fabisiak J.P., Sedlov A., Kagan V.E. // Antioxid. Redox Signal. 2002. V. 4. № 5. P. 855–865.
Tran N.G., Kalyvas H., Skodje K.M., Hayashi T., Moënne-Loccoz P., Callan P.E. et al. // J. Am. Chem. Soc. 2011. V. 133. № 5. P. 1184–1187.
Kosmachevskaya O.V., Nasybullina E.I., Shumaev K.B., Novikova N.N., Topunov A.F. // Appl. Biochem. Microbiol. 2020. V. 56. № 5. P. 512–520.
Akentieva N., Gizatullin A., Sanina N., Shkondina N., Abramova K., Tikhonov V. et al. // Biointerface Res. Appl. Chem. 2023. V. 13. № 4. e344. https://doi.org/10.33263/BRIAC134.344