Skip to main content
SpringerLink
Log in

EPR Characterization of Mononuclear Dinitrosyl Iron Complex with Persulfide as a New Representative of Dinitrosyl Iron Complexes in Biological Systems: an Overview

  • Review
  • Published:
Applied Magnetic Resonance Aims and scope Submit manuscript

Abstract

Some recent data on the presence of mononuclear dinitrosyl iron complexes (M-DNIC) with persulfide (R-S-S−) ligands with a characteristic electron paramagnetic resonance signal at g ⊥ = 2.35 and g || = 2.02 (g aver. = 2.03) in biological systems (e.g., Escherichia coli cells and isolated iron–sulfur proteins) are reviewed. The generation of M-DNIC is controlled by inorganic sulfur (sulfide, S2−) whose binding to thiols gives persulfides. It is suggested that enhanced production of inorganic sulfur is a result of destruction of active centers of iron–sulfur proteins in the presence of NO or NO-containing compounds. Dinitrosyl iron complexes with thiol-containing ligands are the most active participants in this process. Inorganic sulfur may appear in biological systems during the synthesis or resynthesis of active centers of iron–sulfur proteins in response to activation of cysteine desulfurase, the key enzyme in sulfide synthesis from cysteine.

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
Fig. 4
Fig. 5
Scheme 1
Scheme 2

Similar content being viewed by others

References

  1. R.M. Nalbandyan, A.F. Vanin, L.A. Blumenfeld, in Abstracts of the Meeting “Free Radicals Processes in Biological Systems”, Moscow, (1964) p. 18

  2. J.R. Mallard, M. Kent, Nature 204, 1192 (1964)

    Google Scholar 

  3. A.F. Vanin, R.M. Nalbandyan, Biofizika (Rus) 10, 167–168 (1965)

    Google Scholar 

  4. A.J. Vithaythil, J.L. Ternberg, B. Commoner, Nature 207, 1246–1249 (1965)

    Google Scholar 

  5. A.F. Vanin, L.A. Blumenfeld, A.G. Chenverokov, Biofizika (Rus) 12, 829–841 (1967)

    Google Scholar 

  6. E.N. Frolov, A.F. Vanin, Biofizika (Rus) 18, 605–610 (1973)

    Google Scholar 

  7. W.A. Goodman, I.B. Raynor, M.C.R. Simmons, J. Chem. Soc. (A). 2038–2043 (1970)

  8. H. Cruz-Ramos, J. Crack, G. Wu, M.N. Hughes, C. Scott, A.J. Thomson, J. Green, R.K. Poole, EMBO J. 21, 3235–3244 (2002)

    Google Scholar 

  9. J. Crack, L.J. Smith, M.R. Stapleton, J. Peck, N.J. Watmough, M.J. Buttner, R.S. Buxton, V.S. Oganesyan, A.J. Thomson, N.E. Le Brun, J. Am. Chem. Soc. 133, 1112–1121 (2011)

    Google Scholar 

  10. J. Crack, M.R. Stapleton, J. Green, A.J. Thomson, N.E. Le Brun, J. Biol. Chem. 288, 11492–11502 (2013)

    Google Scholar 

  11. I.I. Lobysheva, M.V. Stupakova, V.D. Mikoyan, S.V. Vasilyeva, A.F. Vanin, FEBS Lett. 454, 177–180 (1999)

    Google Scholar 

  12. C.F. Amabile-Cuevas, B. Demple, Nucleic Acids Res. 99, 4479–4484 (1991)

    Google Scholar 

  13. N.V. Voevodskaya, V.A. Serezhenkov, C.E. Cooper, L.N. Kubrina, A.F. Vanin, Biochem. J. 368, 633–639 (2002)

    Google Scholar 

  14. S.V. Vasilyeva, EYu. Moshkovskaya, A.S. Terekhov, V.D. Mikoyan, A.F. Vanin, Russ. J. Genetics 44, 21–26 (2008). (Translation from Genetika)

  15. S.V. Vasilyeva, D.A. Strel`tsova, A.V. Vlaskina, V.D. Mikoyan, A.F. Vanin, Biophysics 57, 166–169 (2012). (Translation from Biofizika)

  16. S.V. Vasilyeva, D.A. Strel`tsova, E.Yu. Moshkovskaya, A.F. Vanin, V.D. Mikoyan, N.A. Sanina, S.M. Aldoshin, Dokl. Biochem. Biophys. 435, 283–286 (2010). (Translation from Doklady Akademii Nauk)

    Google Scholar 

  17. M.V. Stupakova, I.I. Lobysheva, V.D. Mikoyan, A.F. Vanin, S.V. Vasilyeva, Biokhimiya 65(65), 810–816 (2000)

    Google Scholar 

  18. H. Ding, B. Demple, Proc. Natl. Acad. Sci. USA 97, 5146–5150 (2000)

    Google Scholar 

  19. S.V. Vasilyeva, M.V. Stupakova, I.I. Lobysheva, V.D. Mikoyan, A.F. Vanin, Biochemistry (Moscow) 66, 984–988 (2001). (Translation from Biokhimiya)

    Google Scholar 

  20. S.V. Vasilyeva, M.V. Stupakova, I.I. Lobysheva, V.D. Mikoyan, A.F. Vanin, Biokhimiya (Rus) 66, 1209–1214 (2001)

    Google Scholar 

  21. A.F. Vanin, I.V. Malenkova, V.A. Serezhenkov, Nitric Oxide Biol. Chem. 1, 191–203 (1997)

    Google Scholar 

  22. S. Constanzo, S. Menage, R. Purello, R.P. Bonomo, M. Fontecave, Inorg. Chim. Acta. 318, 1–7 (2001)

    Google Scholar 

  23. A.F. Vanin, N.A. Sanina, V.A. Serezhenkov, DSh Burbaev, V.I. Lozinsky, S.M. Aldoshin, Nitric Oxide Biol. Chem. 16, 82–93 (2007)

  24. A.F. Vanin, A.P. Poltorakov, V.D. Mikoyan, L.N. Kubrina, DSh Burbaev, Nitric Oxide Biol. Chem. 23, 1236–1249 (2010)

    Google Scholar 

  25. A.F. Vanin, D.Sh. Burbaev, J. Biophys. 2011, Article ID 878236 (2011)

  26. J.S. Hickok, S. Sahni, H. Shen, A. Arvind, C. Antoniou, L.W.M. Fung, D.D. Thomas, Free Rad. Biol. Med. 51, 1558–1566 (2011)

    Google Scholar 

  27. C.E. Tinberg, Z.J. Tonzetich, H. Wang, L.H. Do, Y. Yoda, S.P. Cramer, S.J. Lippard, J. Am. Chem. Soc. 132, 18168–18176 (2010)

    Google Scholar 

  28. N.P. Tucker, M.G. Hicks, T.A. Clarke, J.C. Crack, G. Chandra, N.E. Le Brun, R. Dixon, M.I. Hutchison, PLoS One 3, e3623 (2008)

  29. R.R. Borodulin, L.N. Kubrina, V.A. Serezhenkov, D.S. Burbaev, V.D. Mikoyan, A. Vanin, Nitric Oxide Biol. Chem. 35, 35–41 (2013)

    Google Scholar 

  30. A.F. Vanin, Nitric Oxide Biol. Chem. 21, 1–13 (2009)

    Google Scholar 

  31. A.F. Vanin, Open Conf. Proc. J. 4, 31–37 (2013)

  32. H. Kimura, N. Shibuya, Y. Kimura, Antioxid. Redox Signal. 17, 45–57 (2012)

    Google Scholar 

  33. Q. Li, J.R. Lancaster, Nitric Oxide Biol. Chem. 35, 21–34 (2013)

    Google Scholar 

Download references

Acknowledgments

This work has been supported by the Russian Foundation for Basic Research (project no. 12-04-00346a) and by the Presidium of the Russian Academy of Sciences within the framework “Fundamental Sciences for Medicine (2013)”.

Author information

Authors and Affiliations

  1. N.N. Semyonov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, Russia

    Anatoly F. Vanin & Vasak D. Mikoyan

  2. N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia

    Svetlana V. Vasilyeva & Darya A. Streltsova

Authors
  1. Anatoly F. Vanin
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Svetlana V. Vasilyeva
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Darya A. Streltsova
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Vasak D. Mikoyan
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Anatoly F. Vanin.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Vanin, A.F., Vasilyeva, S.V., Streltsova, D.A. et al. EPR Characterization of Mononuclear Dinitrosyl Iron Complex with Persulfide as a New Representative of Dinitrosyl Iron Complexes in Biological Systems: an Overview. Appl Magn Reson 45, 375–387 (2014). https://doi.org/10.1007/s00723-014-0523-9

Download citation

  • Received:

  • Revised:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00723-014-0523-9

Keywords

Search

Navigation