Navegar

Colección

Datos Estadísticas

Artículo

Álvarez, L.; Suarez, S.A.; Bikiel, D.E.; Reboucas, J.S.; Batinić-Haberle, I.; Martí, M.A.; Doctorovich, F. "Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps" (2014) Inorganic Chemistry. 53(14):7351-7360
El editor solo permite decargar el artículo en su versión post-print desde el repositorio. Por favor, si usted posee dicha versión, enviela a
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Azanone (1HNO, nitroxyl) is a highly reactive molecule with interesting chemical and biological properties. Like nitric oxide (NO), its main biologically related targets are oxygen, thiols, and metalloproteins, particularly heme proteins. As HNO dimerizes with a rate constant between 106 and 107 M-1 s-1, reactive studies are performed using donors, which are compounds that spontaneously release HNO in solution. In the present work, we studied the reaction mechanism and kinetics of two azanone donors Angelís Salt and toluene sulfohydroxamic acid (TSHA) with eight different Mn porphyrins as trapping agents. These porphyrins differ in their total peripheral charge (positively or negatively charged) and in their MnIII/MnII reduction potential, showing for each case positive (oxidizing) and negative (reducing) values. Our results show that the reduction potential determines the azanone donor reaction mechanism. While oxidizing porphyrins accelerate decomposition of the donor, reducing porphyrins react with free HNO. Our results also shed light into the donor decomposition mechanism using ab initio methods and provide a thorough analysis of which MnP are the best candidates for azanone trapping and quantification experiments. © 2014 American Chemical Society.

Registro:

Documento: Artículo
Título:Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps
Autor:Álvarez, L.; Suarez, S.A.; Bikiel, D.E.; Reboucas, J.S.; Batinić-Haberle, I.; Martí, M.A.; Doctorovich, F.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, INQUIMAE-CONICET, Pab. II (1428), Buenos Aires, Argentina
Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pab. II (1428), Buenos Aires, Argentina
Departamento de Quimica, CCEN, Universidade Federal da Paraiba, Joao Pessoa, Paraiba, Brazil
Department of Radiation Oncology, Duke University Medical School, Durham, NC 27710, United States
Palabras clave:iron; manganese; nitrogen oxide; nitroxyl; porphyrin; chemistry; kinetics; oxidation reduction reaction; Iron; Kinetics; Manganese; Nitrogen Oxides; Oxidation-Reduction; Porphyrins
Año:2014
Volumen:53
Número:14
Página de inicio:7351
Página de fin:7360
DOI: http://dx.doi.org/10.1021/ic5007082
Título revista:Inorganic Chemistry
Título revista abreviado:Inorg. Chem.
ISSN:00201669
CODEN:INOCA
CAS:iron, 14093-02-8, 53858-86-9, 7439-89-6; manganese, 16397-91-4, 7439-96-5; nitrogen oxide, 11104-93-1; porphyrin, 24869-67-8; Iron; Manganese; Nitrogen Oxides; nitroxyl; Porphyrins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v53_n14_p7351_Alvarez

Referencias:

  • Doctorovich, F., Bikiel, D., Pellegrino, J., Suárez, S.A., Larsen, A., Martí, M.A., (2011) Coord. Chem. Rev., 255, pp. 2764-2784
  • Miranda, K., (2005) Coord. Chem. Rev., 249, pp. 433-455
  • Shafirovich, V., Lymar, S.V., (2003) J. Am. Chem. Soc., 125, pp. 6547-6552
  • Paolocci, N., Jackson, M.I., Lopez, B.E., Miranda, K., Tocchetti, C.G., Wink, D.A., Hobbs, A.J., Fukuto, J.M., (2007) Pharmacol. Ther., 113, pp. 442-458
  • 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. 2264-2276
  • Heinecke, J.L., Khin, C., Pereira, J.C.M., Suárez, S.A., Iretskii, A.V., Doctorovich, F., Ford, P.C., (2013) J. Am. Chem. Soc., 135, pp. 4007-4017
  • Simonaitis, R., (1963) J. Phys. Chem., 67, pp. 2227-2228
  • Clyne, M.A.A., Thrush, B.A., (1961) Trans. Faraday Soc., 57, pp. 1305-1314
  • Strausz, O.P., Gunning, H.E., (1964) Trans. Faraday Soc., 60, p. 347
  • Wright, A.M., Wu, G., Hayton, T.W., (2012) J. Am. Chem. Soc., 134, pp. 9930-9933
  • Zheng, S., Berto, T.C., Dahl, E.W., Hoffman, M.B., Speelman, A.L., Lehnert, N., (2013) J. Am. Chem. Soc., 135, pp. 4902-4905
  • Speelman, A.L., Lehnert, N., (2014) Acc. Chem. Res., 47, pp. 1106-1116
  • Sabat, J., Egawa, T., Lu, C., Stuehr, D.J., Gerfen, G.J., Rousseau, D.L., Yeh, S.-R., (2013) J. Biol. Chem., 288, pp. 6095-6106
  • Ford, P.C.P.C., Lorkovic, I.M.I.M., (2002) Chem. Rev., 102, pp. 993-1018
  • Franke, A., Suzuki, N., Higuchi, T., Okuzono, K., Eldik, R.V., Chemistry, F., (2005) World, pp. 5360-5375
  • Roncaroli, F., Eldik, R.V., (2006) J. Am. Chem. Soc., 128, pp. 8042-8053
  • Martí, M.A., Bari, S.E., Estrin, D.A., Doctorovich, F., (2005) J. Am. Chem. Soc., 127, pp. 4680-4684
  • Guillaud, G., (1998) Coord. Chem. Rev., pp. 1433-1484
  • Lehnert, N., Scheidt, W.R., Wolf, M.W., (2014) Struct. & Bonding, 154, pp. 155-224
  • Farmer, P.J., Sulc, F., (2005) J. Inorg. Biochem., 99, pp. 166-184
  • Lin, R., Farmer, P.J., (2000) J. Am. Chem. Soc., 122, pp. 2393-2394
  • Immoos, C.E., Sulc, F., Farmer, P.J., Czarnecki, K., Bocian, D.F., Levina, A., Aitken, J.B., Lay, P.A., (2005) J. Am. Chem. Soc., 127, pp. 814-815
  • Bari, S.E., Martí, M.A., Amorebieta, V.T., Estrin, D.A., Doctorovich, F., (2003) J. Am. Chem. Soc., 125, pp. 15272-15273
  • Pellegrino, J., Bari, S.E., Bikiel, D.E., Doctorovich, F., (2010) J. Am. Chem. Soc., 132, pp. 989-995
  • Goodrich, L.E., Roy, S., Alp, E.E., Zhao, J., Hu, M.Y., Lehnert, N., (2013) Inorg. Chem., 52, pp. 7766-7780
  • Kurtikyan, T.S., Gulyan, G.M., Martirosyan, G.G., Lim, M.D., Ford, P.C., (2005) J. Am. Chem. Soc., 127, pp. 6216-6224
  • Møller, J.K.S., Skibsted, L.H., (2004) Chemistry, 10, pp. 2291-2300
  • Suárez, S.A., Martí, M.A., De Biase, P.M., Bari, S.E., Doctorovich, F., (2007) Polyhedron, 26, pp. 4673-4679
  • Spasojevic, I., Batini-Haberle, I., Fridovich, I., (2000) Nitric Oxide, 4, pp. 526-533
  • 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, pp. 9196-9201
  • Bonner, F.T., Degani, H., Akhtar, M.J., (1981) J. Am. Chem. Soc., 103, pp. 3739-3742
  • Batinic-Haberle, I., Spasojevic, I., Hambright, P., Benov, L., Crumbliss, A.L., Fridovich, I., (1999) Inorg. Chem., 38, pp. 4011-4022
  • Ferrer-Sueta, G., Hannibal, L., Batinic-Haberle, I., Radi, R., (2006) Free Radical Biol. Med., 41, pp. 503-512
  • Batinic-Haberle, I., Spasojevic, I., Tse, H., Tovmasyan, A., St. Clair, D.K., Vujaskovic, Z., Dewhirst, M.D., Piganelli, J.D., (2012) Amino Acids, 42, pp. 95-113
  • Rebouças, J.S., Spasojević, I., Batinić-Haberle, I., (2008) J. Biol. Inorg. Chem., 13, pp. 289-302
  • Delmastro-Greenwood, M.M., Votyakova, T., Goetzman, E., Marre, M.L., Previte, D.M., Tovmasyan, A., Batinic-Haberle, I., Piganelli, J.D., (2013) Antioxid. Redox Signaling, 19, pp. 1902-1915
  • Batinic-Haberle, I., Tovmasyan, A., Spasojevic, I., (2013) Bioinorg. React. Mech., 9, pp. 35-58
  • Seel, F., Bliefert, C., (1972) Z. Anorg. Allg. Chem., 394, pp. 187-196
  • Hughes, M., Cammack, R., (1999) Methods Enzymol., 301, pp. 279-287
  • Hughes, M.N., Wimbledon, P.E., (1976) J. Chem. Soc., Dalton Trans., 8, pp. 703-707
  • Suárez, S., Bikiel, D., Wetzler, D., Martí, M.A., Doctorovich, F., (2013) Anal. Chem., 85, pp. 10262-10269
  • Suárez, S.A., Fonticelli, M.H., Rubert, A.A., De La Llave, E., Scherlis, D., Salvarezza, R.C., Martí, M.A., Doctorovich, F., (2010) Inorg. Chem., 49, pp. 6955-6966
  • Dutton, A.S., Fukuto, J.M., Houk, K.N., (2004) J. Am. Chem. Soc., 126, pp. 3795-3800
  • Sirsalmath, K., Suárez, S.A., Bikiel, D.E., Doctorovich, F., (2013) J. Inorg. Biochem., 118, pp. 134-139
  • Laverman, L.E., Ford, P.C., (2001) J. Am. Chem. Soc., 123, pp. 11614-11622
  • Boron, I., Suárez, S.A., Doctorovich, F., Martí, M.A., Bari, S.E., (2011) J. Inorg. Biochem., 105, pp. 1044-1049
  • Torras, J., Seabra, G., Roitberg, A., (2009) J. Chem. Theory, 5, pp. 37-46
  • Liang, J.-L., Huang, J.-S., Zhou, Z.-Y., Cheung, K.K., Che, C.-M., (2001) Chem.-Eur. J., 7, pp. 2306-2317
  • Crotti, C., Sishta, C., Pacheco, A., James, B.R., (1988) Inorg. Chim. Acta, 141, pp. 13-15
  • Ti, G.-B., Khan, M.A., Richter-Addo, G.B., (1996) Inorg. Chem., 35, pp. 3453-3554
  • Leitão, E.F.V., Ventura, E., Santana, O.L., Do Monte, S.A., (2014) Int. J. Quantum Chem., , 10.1002/qua.24595
  • Xu, N., Goodrich, L.E., Lehnert, N., Powell, D.R., Richter-Addo, G.B., (2010) Inorg. Chem., 49, pp. 4405-4419
  • Farmer, P., Kumar, M., Almaraz, E., (2010) Comments Inorg. Chem., 31, pp. 130-143
  • Sulc, F., Immoos, C.E., Pervitsky, D., Farmer, P.J., (2004) J. Am. Chem. Soc., 126, pp. 1096-1101
  • Lim, M.D., Lorkovic, I.M., Ford, P.C., (2005) J. Inorg. Biochem., 99, pp. 151-165
  • Miranda, K.M., (2005) Coord. Chem. Rev., 249, pp. 433-455
  • Bartberger, M.D., Fukuto, J.M., Houk, K.N., (2001) Proc. Natl. Acad. Sci. U.S.A., 98, pp. 2194-2198
  • Liochev, S.I., Fridovich, I., (2003) Free Radical Biol. Med., 34, pp. 1399-1404
  • Lymar, S.V., Shafirovich, V., Poskrebyshev, G.A., (2005) Inorg. Chem., 44, pp. 5212-5221
  • Sharma, V.S., Isaacson, R.A., John, M.E., Waterman, M.R., Chevion, M., (1983) Biochemistry, 22, pp. 3897-3902
  • Scott, E.E., Gibson, Q.H., Olson, J.S., (2001) J. Biol. Chem., 276, pp. 5177-5188

Citas:

---------- APA ----------
Álvarez, L., Suarez, S.A., Bikiel, D.E., Reboucas, J.S., Batinić-Haberle, I., Martí, M.A. & Doctorovich, F. (2014) . Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps. Inorganic Chemistry, 53(14), 7351-7360.
http://dx.doi.org/10.1021/ic5007082
---------- CHICAGO ----------
Álvarez, L., Suarez, S.A., Bikiel, D.E., Reboucas, J.S., Batinić-Haberle, I., Martí, M.A., et al. "Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps" . Inorganic Chemistry 53, no. 14 (2014) : 7351-7360.
http://dx.doi.org/10.1021/ic5007082
---------- MLA ----------
Álvarez, L., Suarez, S.A., Bikiel, D.E., Reboucas, J.S., Batinić-Haberle, I., Martí, M.A., et al. "Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps" . Inorganic Chemistry, vol. 53, no. 14, 2014, pp. 7351-7360.
http://dx.doi.org/10.1021/ic5007082
---------- VANCOUVER ----------
Álvarez, L., Suarez, S.A., Bikiel, D.E., Reboucas, J.S., Batinić-Haberle, I., Martí, M.A., et al. Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: Defining the better traps. Inorg. Chem. 2014;53(14):7351-7360.
http://dx.doi.org/10.1021/ic5007082