Skip to main content
SpringerLink
Log in

Effect of Dinitrosyl Iron Complex on Albumin Conformation

  • SHORT COMMUNICATION
  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

Binding of dinitrosyl iron complex (DNIC) to albumin was studied using time-resolved fluorescence (TRF) and electron spin resonance (ESR) spectroscopy. It was found that the fluorescence lifetime of bovine serum albumin (BSA) and human serum albumin (HSA) decreases with binding and depends on DNIC concentration. The observed biexponential pattern of the BSA tryptophan (Trp) fluorescence decay is explained by the presence of two tryptophan residues in the protein molecule. We believe that DNIC forms stable complexes with the cysteine (Cys34) residue in the domain I of albumin. It was shown that the lifetime of albumin tryptophan fluorescence decreased during co-incubation of BSA with DNICs and glutathione. Effects of DNIC on the binding of specific spin-labeled fatty acids with albumin in human blood plasma were studied in vitro. The presence of DNIC in blood plasma does not change conformation of albumin domains II and III. We suggest that the most possible interaction between DNICs and albumin is the formation of a complex; and nitrosylation of the cysteine residue in the albumin domain I occurs without the changes in albumin conformation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1.
Fig. 2.
Fig. 3.

Abbreviations

BSA:

bovine serum albumin

DNIC:

dinitrosyl iron complex

ESR:

electron spin resonance

GS-NO:

S-nitroso glutathione

HAS:

human serum albumin

TRF:

time-resolved fluorescence

References

  1. De Souza, T. C. F., Périssé, A. R. S., and Moura, M. (2015) Noise exposure and hypertension: investigation of a silent relationship, BMC Public Health, 15, 328.

    Article  Google Scholar 

  2. Diao, D., Wright, J. M., Cundiff, D. K., and Gueyffier, F. (2012) Pharmacotherapy for mild hypertension, Cochrane Database Syst. Rev., 8, CD006742.

    Google Scholar 

  3. Lundberg, J. O., Weitzberg, E., and Gladwin, M. T. (2008) The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics, Nat. Rev. Drug Discov., 7, 156.

    Article  CAS  Google Scholar 

  4. Broniowska, K. A., Diers, A. R., and Hogg, N. (2013) S-nitrosoglutathione, Biochim. Biophys. Acta, 5, 3173-3181.

    Article  Google Scholar 

  5. Liu, T., Zhang, M., Terry, M. H., Schroeder, H., Wilson, S., et al. (2018) Hemodynamic effects of glutathione-liganded binuclear dinitrosyl iron complex: evidence for nitroxyl generation and modulation by plasma albumin, Mol. Pharmacol., 5, 427-437.

    Article  Google Scholar 

  6. Chazov, E. I., Rodnenkov, O. V., Zorin, A. V., Lakomkin, V. L., Gramovich, V. V., et al. (2012) Hypotensive effect of Oxacom® containing a dinitrosyl iron complex with glutathione: animal studies and clinical trials on healthy volunteers, Nitric Oxide, 26, 148-156.

    Article  CAS  Google Scholar 

  7. Gow, A. J., Buerk, D. G., and Ischiropoulos, H. (1997) A novel reaction mechanism for the formation of S-nitrosothiol in vivo, J. Biol. Chem., 5, 2841-2845.

    Article  Google Scholar 

  8. Lakomkin, V. L., Vanin, A. F., Timoshin, A. A., Kapelko, V. I., and Chazov, E. I. (2007) Long-lasting hypotensive action of stable preparations of dinitrosyl-iron complexes with thiol-containing ligands in conscious normotensive and hypertensive rats, Nitric Oxide, 16, 413-418.

    Article  CAS  Google Scholar 

  9. Liu, X., Miller, M. J., Joshi, M. S., Thomas, D. D., and Lancaster, J. R., Jr. (1998) Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes, Proc. Natl. Acad. Sci. USA, 95, 2175-2179.

    Article  CAS  Google Scholar 

  10. Moller, M. N., Li, Q., Vitturi, D. A., Robinson, J. M., Lancaster, J. R., and Denicola, A. (2007) Membrane “lens” effect: focusing the formation of reactive nitrogen oxides from the NO/O2 reaction, Chem. Res. Toxicol., 20, 709-714.

    Article  Google Scholar 

  11. Burstein, A., Vedenkina, N. S., and Ivkova, M. N. (1973) Fluorescence and the location of tryptophan residues in protein molecules, Photochem. Photobiol., 18, 263-279.

    Article  CAS  Google Scholar 

  12. Birkett, D. J., Myers, S. P., and Sudlow, G. (1977) Effects of fatty acids on two specific drug binding sites on human serum albumin, Mol. Pharmacol., 13, 987-992.

    CAS  PubMed  Google Scholar 

  13. Zhang, Y. Y., Xu, A. M., Nomen, M., Walsh, M., Keaney, J. F. Jr., and Loscalzo, J. (1996) Nitrosation of tryptophan residue(s) in serum albumin and model dipeptides. Biochemical characterization and bioactivity, J. Biol. Chem., 271, 14271-14279.

    Article  CAS  Google Scholar 

  14. Borodulin, R. R., Kubrina, L. N., Serezhenkov, V. A., Burbaev, D. S., Mikoyan, V. D., and Vanin, A. F. (2013) Redox conversions of dinitrosyl iron complexes with natural thiol-containing ligands, Nitric Oxide, 35, 35-41.

    Article  CAS  Google Scholar 

  15. Kazmierczak, S. C., Gurachevsky, A., Matthes, G., and Muravsky, V. (2006) Electron spin resonance spectroscopy of serum albumin: a novel new test for cancer diagnosis and monitoring, Clin. Chem., 52, 2129-2134.

    Article  CAS  Google Scholar 

  16. Alcala, J. R., Gratton, E., and Prendergast, F. G. (1987) Fluorescence lifetime distributions in proteins, Biophys. J., 51, 597-604.

    Article  CAS  Google Scholar 

  17. Yukio, Y., and Jiro, T. (1972) Polarized absorption spectra of crystals of indole and its related compounds, Bull. Chem. Soc. Japan, 45, 1362-1366.

    Article  Google Scholar 

  18. Amar, B. T. G., and Sang, J. C. (2014) Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Förster resonance energy transfer techniques, Int. J. Mol. Sci., 15, 22518-22538.

    Article  Google Scholar 

  19. Lakowicz, J. (2007) Principles of Fluorescence Spectroscopy, Springer, New York, 3rd Edn.

  20. Zhdanova, N. G., Shirshin, E. A., Maksimov, E. G., Panchishin, I. M., Saletsky, A. M., and Fadeev, V. V., (2015) Tyrosine fluorescence probing of surfactant-induced conformational changes of albumin, Photochem. Photobiol. Sci., 14, 897-908.

    Article  CAS  Google Scholar 

  21. Anand, U., Jash, C., and Mukherjee, S. (2010) Spectroscopic probing of the microenvironment in a protein-surfactant assembly, J. Phys. Chem. B, 114, 15839-15845.

    Article  CAS  Google Scholar 

  22. Boese, M., Mordvintcev, P., Vanin, A. F., Busse, R., and Mülsch, A. (1995) S-Nitrosation of serum albumin by dinitrosyl–iron complex, J. Biol. Chem., 270, 29244-29249.

    Article  CAS  Google Scholar 

  23. Vanin, A. F., Lozinsky, V. I., and Kapel’ko, V. I. (2005) Polymeric composition for designing a stabilized form of dinitrosyl–iron complex and the method of this complex form synthesis, Russ. Pat., No. 2,291,880.

  24. Noble, D. R., Swift, H. R., and Williams, D. L. H. (1999) Nitric oxide release from S-nitrosoglutathione (GSNO), Chem. Commun., 22, 2317-2318.

    Article  Google Scholar 

  25. Gelamo, E. L., and Tabak, M. (2000) Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants, Spectrochim. Acta Part A, 56, 2255-2271.

    Article  Google Scholar 

Download references

Acknowledgments

The authors are grateful to Dr. Margarita Rodionova for her invaluable help in preparation of the manuscript.

Funding

This study was financially supported by the Russian Science Foundation (grant no. 19-79-30062, for M.G.V. and Y.A.I.) as well as by the Interdisciplinary Scientific and Educational School of Moscow University “Molecular Technologies of Living Systems and Synthetic Biology”.

Author information

Authors and Affiliations

  1. Faculty of Biology, Lomonosov Moscow State University, 119991, Moscow, Russia

    Elvin S. Allakhverdiev, Georgy V. Maksimov, Oksana G. Luneva, Georgy V. Tsoraev & Alexander I. Yusipovich

  2. Russian National Medical Research Center of Cardiology, 121552, Moscow, Russia

    Elvin S. Allakhverdiev, Oleg V. Rodnenkov & Tamila V. Martynyuk

  3. Federal State Autonomous Educational Institution of Higher Education “National Research Technological University “MISIS”, 119049, Moscow, Russia

    Georgy V. Maksimov & Aleksey D. Ivanov

Authors
  1. Elvin S. Allakhverdiev
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Georgy V. Maksimov
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Oleg V. Rodnenkov
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Oksana G. Luneva
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Georgy V. Tsoraev
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Aleksey D. Ivanov
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Alexander I. Yusipovich
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. Tamila V. Martynyuk
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Elvin S. Allakhverdiev or Georgy V. Maksimov.

Ethics declarations

The authors declare no conflicts of interest in financial or any other sphere. All procedures performed in studies involving human participants were in accordance with the ethical standards of the institutional and/or national research committee and with the 1964 Helsinki declaration and its later amendments or comparable ethical standards.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Allakhverdiev, E.S., Maksimov, G.V., Rodnenkov, O.V. et al. Effect of Dinitrosyl Iron Complex on Albumin Conformation. Biochemistry Moscow 86, 533–539 (2021). https://doi.org/10.1134/S0006297921050023

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S0006297921050023

Keywords

Search

Navigation