Advertisement

Biochemistry (Moscow)

, Volume 73, Issue 1, pp 92–96 | Cite as

Mechanism of inhibition of catalase by nitro and nitroso compounds

  • V. Yu. TitovEmail author
  • Yu. M. Petrenko
  • A. F. Vanin
Article

Abstract

Dinitrosyl iron complexes (DNIC) with thiolate ligands and S-nitrosothiols, which are NO and NO+ donors, share the earlier demonstrated ability of nitrite for inhibition of catalase. The efficiency of inhibition sharply (by several orders in concentration of these agents) increases in the presence of chloride, bromide, and thiocyanate. The nitro compounds tested—nitroarginine, nitroglycerol, nitrophenol, and furazolidone—gained the same inhibition ability after incubation with ferrous ions and thiols. This is probably the result of their transformation into DNIC. None of these substances lost the inhibitory effect in the presence of the well known NO scavenger oxyhemoglobin. This fact suggests that NO+ ions rather than neutral NO molecules are responsible for the enzyme inactivation due to nitrosation of its structures. The enhancement of catalase inhibition in the presence of halide ions and thiocyanate might be caused by nitrosyl halide formation. The latter protected nitrosonium ions against hydrolysis, thereby ensuring their transfer to the targets in enzyme molecules. The addition of oxyhemoglobin plus iron chelator o-phenanthroline destroying DNIC sharply attenuated the inhibitory effect of DNIC on catalase. o-Phenanthroline added alone did not influence this effect. Oxyhemoglobin is suggested to scavenge nitrosonium ions released from decomposing DNIC, thereby preventing catalase nitrosation. The mixture of oxyhemoglobin and o-phenanthroline did not affect the inhibitory action of nitrite or S-nitrosothiols on catalase.

Key words

dinitrosyl iron complex (DNIC) nitro compounds nitroso compounds catalase inhibition 

Abbreviations

Cys-NO

S-nitrosocysteine

DNIC-GS

dinitrosyl iron complex with glutathione

GSH

glutathione

GS-NO

S-nitrosoglutathione

HbO2

oxyhemoglobin

p-NP

p-nitrophenol

o-Ph

o-phenanthroline

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Cohen, G., Martinez, M., and Hochstein, P. (1964) Biochemistry, 3, 901–903.CrossRefPubMedGoogle Scholar
  2. 2.
    Nicholls, P. (1965) Biochim. Biophys. Acta, 99, 286–297.PubMedGoogle Scholar
  3. 3.
    Young, L., and Siegel, L. (1988) Biochemistry, 27, 2790–2800.CrossRefPubMedGoogle Scholar
  4. 4.
    Titov, V. (2006) Current Enzyme Inhibition, 2, 1–17.CrossRefGoogle Scholar
  5. 5.
    Titov, V. Yu., and Petrenko, Yu. M. (2003) Biochemistry (Moscow), 68, 627–633.CrossRefGoogle Scholar
  6. 6.
    Brown, G. (1995) Eur. J. Biochem., 232, 188–191.CrossRefPubMedGoogle Scholar
  7. 7.
    Licht, W., Tannenbaum, S., and Deen, W. (1988) Carcinogenesis, 9, 365–372.CrossRefPubMedGoogle Scholar
  8. 8.
    Licht, W., Fox, J., and Deen, W. (1988) Carcinogenesis, 9, 373–377.CrossRefPubMedGoogle Scholar
  9. 9.
    Mirvish, S. (1975) Toxicol. Appl. Pharmacol., 31, 325–351.CrossRefPubMedGoogle Scholar
  10. 10.
    Severina, I., Bussygina, O., Pyatakova, N., Malenkova, I., and Vanin, A. (2003) Nitric Oxide, 8, 155–163.CrossRefPubMedGoogle Scholar
  11. 11.
    Balazy, M., Kaminski, P., Mao, K., Tan, J., and Wolin, M. (1998) J. Biol. Chem., 273, 32009–32015.CrossRefPubMedGoogle Scholar
  12. 12.
    Titov, V. Yu., and Petrenko, Yu. M. (2005) Biochemistry (Moscow), 70, 473–483.CrossRefGoogle Scholar
  13. 13.
    Titov, V., Vanin, A., Serezhenkov, V., and Petrenko, Yu. (2003) Probl. Ecol. Secur. Agric., 6, 50–65.Google Scholar
  14. 14.
    Kurbanov, I. S., Mordvintsev, P. I., Aliev, D. I., and Vanin, A. F. (1989) Vopr. Med. Khim., 35, 87–91.PubMedGoogle Scholar
  15. 15.
    Vanin, A., Muller, B., Alencar, J., Lobysheva, I., Nepveu, F., and Stoclet, J.-C. (2002) Nitric Oxide, 7, 194–209.CrossRefPubMedGoogle Scholar
  16. 16.
    Vanin, A. F., Papina, A. A., Serezhenkov, V. A., and Koppenol, W. H. (2004) Nitric Oxide, 10, 60–73.CrossRefPubMedGoogle Scholar
  17. 17.
    Vanin, A. F. (1993) Biofizika, 38, 751–761.PubMedGoogle Scholar
  18. 18.
    Boese, M., Mordvintcev, P. I., Vanin, A. F., Busse, R., and Mulsch, A. (1995) J. Biol. Chem., 270, 29244–29249.CrossRefPubMedGoogle Scholar
  19. 19.
    Deisseroth, A., and Dounce, A. (1970) Physiol. Rev., 50, 319–375.PubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  1. 1.Russian Medical State UniversityMoscowRussia
  2. 2.Semenov Institute of Chemical PhysicsRussian Academy of SciencesMoscowRussia

Personalised recommendations