Navegar

Colección

Datos Estadísticas

Artículo

Suárez, S.A.; Martí, M.A.; De Biase, P.M.; Estrin, D.A.; Bari, S.E.; Doctorovich, F. "HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes" (2007) Polyhedron. 26(16):4673-4679
Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

The role of nitric oxide (NO) as a signalling molecule in biological systems has been thoroughly studied in the last decades. More recently, there has been an increasing interest in the one-electron reduction product of NO, namely nitroxyl (HNO/NO-). Some studies suggest that nitroxyl can be produced by nitric oxide synthases under certain conditions, and that distinct pharmacological effects are observed for NO and nitroxyl donors. HNO is capable of react with heme proteins, thiols, molecular oxygen, NO and HNO itself. However, only recently the different reactivity patterns are being thoroughly understood. Heme model compounds offer the opportunity to study the reaction kinetics without the complexity arising from ligand interactions with the protein matrix. In this study we analyzed the reaction between the commonly used nitroxyl donors sodium trioxodinitrate and toluene sulfohydroxamic acid, with the ferric model compounds microperoxidase-11 (MP11) and the cationic metalloporphyrin [FeIIITEPyP]5+ (Tetrakis N-ethylpyridinium-2yl porphyne). Our results show that there are two alternative modes of reactivity for nitroxyl donors towards heme in aqueous solutions. The first one comprises the heme assisted decomposition of the donor, enhancing its decomposition rate more than 100-fold. In the second, the donor produces HNO which subsequently reacts with the porphyrin. The observed rate constants (of about 105 M-1 s-1) are consistent with the estimated data for the HNO reaction with heme proteins, and may be controlled by the leaving water ligand. This rate constant probably represents an upper limit for the bimolecular rate constant of HNO towards these proteins. © 2007 Elsevier Ltd. All rights reserved.

Registro:

Documento: Artículo
Título:HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes
Autor:Suárez, S.A.; Martí, M.A.; De Biase, P.M.; Estrin, D.A.; Bari, S.E.; Doctorovich, F.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE, CONICET, Pabellón II, Buenos Aires C1428EHA, Argentina
Palabras clave:Ferric porphyrin; Heme; HNO; HNO donor; Kinetics; Microperoxidase; Nitroxyl
Año:2007
Volumen:26
Número:16
Página de inicio:4673
Página de fin:4679
DOI: http://dx.doi.org/10.1016/j.poly.2007.05.040
Título revista:Polyhedron
Título revista abreviado:Polyhedron
ISSN:02775387
CODEN:PLYHD
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02775387_v26_n16_p4673_Suarez

Referencias:

  • Hobbs, A.J., Fukuto, J.M., Ignarro, L.J., (1994) Proc. Natl. Acad. Sci. U.S.A., 91, p. 10992
  • Schmidt, H.H.H.W., Hofmann, H., Schindler, U., Shutenko, Z.S., Cunningham, D.D., Feelisch, M., (1996) Proc. Natl. Acad. Sci. U.S.A., 93, p. 14492
  • Adak, S., Wang, Q., Stuehr, D.J., (2000) J. Biol. Chem., 275, p. 33554
  • Pagliaro, P., (2003) Life Sci., 73, p. 2137
  • Wink, D.A., Miranda, K.M., Katori, T., Mancardi, D., Thomas, D.D., Ridnour, L., Espey, M.G., Paolocci, N., (2003) Am. J. Physiol. Heart Circ. Physiol., 285, pp. H2264
  • Pagliaro, P., Mancardi, D., Rastaldo, R., Penna, C., Gattullo, D., Miranda, K.M., Feelisch, M., Paolocci, N., (2003) Free Radical Biol. Med., 34, p. 33
  • Paolocci, N., Katori, T., Champion, H.C., St John, M.E., Miranda, K.M., Fukuto, J.M., Wink, D.A., Kass, D.A., (2003) Proc. Natl. Acad. Sci. U.S.A., 100, p. 5537
  • Bazylinski, D.A., Hollocher, T.C., (1985) J. Am. Chem. Soc., 107, p. 7982
  • Bazylinski, D.A., Goretski, J., Hollocher, T.C., (1985) J. Am. Chem. Soc., 107, p. 7986
  • Doyle, M.P., Mahapatro, S.N., Broene, R.D., Guy, J.K., (1988) J. Am. Chem. Soc., 110, p. 593
  • Miranda, K.M., Nims, R.W., Thomasa, D.D., Espey, M.G., Citrin, D., Bartberger, M.D., Paolocci, N., Wink, D.A., (2003) J. Inorg. Biochem., 93, p. 52
  • Sulc, F., Immoos, C.E., Pervitsky, D., Farmer, P.J., (2004) J. Am. Chem. Soc., 126, p. 1096
  • Bari, S.E., Marti, M.A., Amorebieta, V.T., Estrin, D.A., Doctorovich, F., (2003) J. Am. Chem. Soc., 125, p. 15272
  • Wong, P.S.Y., Hyun, J., Fukuto, J.M., Shirota, F.N., DeMaster, E.G., Shoeman, D.W., Nagasawa, H.T., (1998) Biochemistry, 37, p. 5362
  • Shafirovich, V., Lymar, S.V., (2002) Proc. Natl. Acad. Sci. U.S.A., 99, p. 7340
  • Miranda, K.M., Paolocci, N., Katori, T., Thomas, D.D., Ford, E., Bartberger, M.D., Espey, M.G., Wink, D.A., (2003) Proc. Natl. Acad. Sci. U.S.A., 100, p. 9196
  • Marti, M.A., Bari, S.E., Estrin, D.A., Doctorovich, F., (2005) J. Am. Chem. Soc., 127, p. 4680
  • Bazylinski, D.A., Hollocher, T.C., (1985) Inorg. Chem., 24, p. 4285
  • Dutton, A.S., Fukuto, J.M., Houk, K.N., (2004) J. Am. Chem. Soc., 126, p. 3795
  • Bonner, F.T., Ko, Y.H., (1992) Inorg. Chem., 31, p. 2514
  • Seel, F., Bliefert, C., (1972) Z. Anorg. Allg. Chem., 394, p. 187
  • Hughes, M.N., Cammack, R., (1999) Nitric Oxide, Pt C, 301, p. 279
  • Hughes, M.N., Wimbledon, P.E., (1976) J. Chem. Soc., Dalton Trans., p. 703
  • Bonner, F.T., Ravid, B., (1975) Inorg. Chem., 14, p. 558
  • Akhtar, M.J., Lutz, C.A., Bonner, F.T., (1979) Inorg. Chem., 18, p. 2369
  • Soler, J.M., Artacho, E., Gale, J.D., Garcia, A., Junquera, J., Ordejon, P., Sanchez-Portal, D., (2002) J. Phys. Condens. Matter, 14, p. 2745
  • Reich, S., Thomsen, C., Ordejon, P., (2002) Phys. Rev. B, 65, p. 155411
  • Troullier, N., Martins, J.L., (1991) Phys. Rev. B, 43, p. 1993
  • Louie, S.G., Froyen, S., Cohen, M.L., (1982) Phys. Rev. B, 26, p. 1738
  • Perdew, J.P., Burke, K., Ernzerhof, M., (1996) Phys. Rev. Lett., 77, p. 3865
  • Capece, L., Marti, M.A., Crespo, A., Doctorovich, F., Estrin, D.A., (2006) J. Am. Chem. Soc., 128, p. 12455
  • Crespo, A., Marti, M.A., Kalko, S.G., Morreale, A., Orozco, M., Gelpi, J.L., Luque, F.J., Estrin, D.A., (2005) J. Am. Chem. Soc., 127, p. 4433
  • NMR and EPR (2000) The Porphyrin Handbook, , Kadish K.M., Smith K.M., and Guilard R. (Eds), Academic Press, San Diego
  • Wilkins, P.C., Jacobs, H.K., Johnson, M.D., Gopalan, A.S., (2004) Inorg. Chem., 43, p. 7877
  • Shibata, Y., Sato, H., Sagami, I., Shimizu, T., (1997) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1343, p. 67
  • Sharma, V.S., Isaacson, R.A., John, M.E., Waterman, M.R., Chevion, M., (1983) Biochemistry, 22, p. 3897
  • Laverman, L.E., Ford, P.C., (2001) J. Am. Chem. Soc., 123, p. 11614
  • Scott, E.E., Gibson, Q.H., Olson, J.S., (2001) J. Biol. Chem., 276, p. 5177

Citas:

---------- APA ----------
Suárez, S.A., Martí, M.A., De Biase, P.M., Estrin, D.A., Bari, S.E. & Doctorovich, F. (2007) . HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes. Polyhedron, 26(16), 4673-4679.
http://dx.doi.org/10.1016/j.poly.2007.05.040
---------- CHICAGO ----------
Suárez, S.A., Martí, M.A., De Biase, P.M., Estrin, D.A., Bari, S.E., Doctorovich, F. "HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes" . Polyhedron 26, no. 16 (2007) : 4673-4679.
http://dx.doi.org/10.1016/j.poly.2007.05.040
---------- MLA ----------
Suárez, S.A., Martí, M.A., De Biase, P.M., Estrin, D.A., Bari, S.E., Doctorovich, F. "HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes" . Polyhedron, vol. 26, no. 16, 2007, pp. 4673-4679.
http://dx.doi.org/10.1016/j.poly.2007.05.040
---------- VANCOUVER ----------
Suárez, S.A., Martí, M.A., De Biase, P.M., Estrin, D.A., Bari, S.E., Doctorovich, F. HNO trapping and assisted decomposition of nitroxyl donors by ferric hemes. Polyhedron. 2007;26(16):4673-4679.
http://dx.doi.org/10.1016/j.poly.2007.05.040