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Referencias:

• Fridovich, I., Superoxide radical and superoxide dismutases (1995) Annu. Rev. Biochem., 64, pp. 97-112
• Stallings, W.C., Pattridge, K.A., Strong, R.K., Ludwig, M.L., Manganese and iron superoxide dismutases are structural homologs (1984) J. Biol. Chem., 259, pp. 10695-10699
• Ismail, S.O., Paramchuk, W., Skeiky, Y.A., Reed, S.G., Bhatia, A., Gedamu, L., Molecular cloning and characterization of two iron superoxide dismutase cdnas from trypanosoma cruzi (1997) Mol. Biochem. Parasitol., 86, pp. 187-197
• Temperton, N.J., Wilkinson, S.R., Kelly, J.M., Cloning of an fe-superoxide dismutase gene homologue from trypanosoma cruzi (1996) Mol. Biochem. Parasitol., 76, pp. 339-343
• Urbina, J.A., Specific chemotherapy of chagas disease: Relevance, current limitations and new approaches (2010) Acta Trop., 115, pp. 55-68
• Lepesheva, G.I., Villalta, F., Waterman, M.R., Targeting trypanosoma cruzi sterol 14-demethylase (cyp51 (2011) Adv. Parasitol., 75, pp. 65-87
• Piacenza, L., Zago, M.P., Peluffo, G., Alvarez, M.N., Basombrio, M.A., Radi, R., Enzymes of the antioxidant network as novel determiners of trypanosoma cruzi virulence (2009) Int. J. Parasitol., 39, pp. 1455-1464
• Kierszenbaum, F., Knecht, E., Budzko, D.B., Pizzimenti, M.C., Phagocytosis: A defense mechanism against infection with trypanosoma cruzi (1974) J. Immunol., 112, pp. 1839-1844
• Munoz-Fernández, M.A., Fernández, M.A., Fresno, M., Synergism between tumor necrosis factor- and interferon- on macrophage activation for the killing of intracellular trypanosoma cruzi through a nitric oxide-dependent mechanism (1992) Eur. J. Immunol., 22, pp. 301-307
• Alvarez, M.N., Peluffo, G., Piacenza, L., Radi, R., Intraphagosomal peroxynitrite as a macrophage-derived cytotoxin against internalized trypanosoma cruzi: Consequences for oxidative killing and role of microbial peroxiredoxins in infectivity (2011) J. Biol. Chem., 286, pp. 6627-6640
• Valez, V., Cassina, A., Batinic-Haberle, I., Kalyanaraman, B., Ferrer-Sueta, G., Radi, R., Peroxynitrite formation in nitric oxide-exposed submitochondrial particles: Detection, oxidative damage and catalytic removal by mn-porphyrins (2013) Arch. Biochem. Biophys., 529, pp. 45-54
• Piacenza, L., Irigoín, F., Alvarez, M.N., Peluffo, G., Taylor, M.C., Kelly, J.M., Wilkinson, S.R., Radi, R., Mitochondrial superoxide radicals mediate programmed cell death in trypanosoma cruzi: Cytoprotective action of mitochondrial iron superoxide dismutase overexpression (2007) Biochem. J., 403, pp. 323-334
• Demicheli, V., Quijano, C., Alvarez, B., Radi, R., Inactivation and nitration of human superoxide dismutase (sod) by fluxes of nitric oxide and superoxide (2007) Free Radic. Biol. Med., 42, pp. 1359-1368
• MacMillan-Crow, L., Crow, J., Kerby, J., Beckman, J., Thompson, J., Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts (1996) Proc. Natl. Acad. Sci. U.S.A., 93, pp. 11853-11858
• Radi, R., Rodriguez, M., Castro, L., Telleri, R., Inhibition of mitochondrial electron transport by peroxynitrite (1994) Arch. Biochem. Biophys., 308, pp. 89-95
• Ghafourifar, P., Schenk, U., Klein, S.D., Richter, C., Mitochondrial nitric-oxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation (1999) J. Biol. Chem., 274, pp. 31185-31188
• Yamakura, F., Taka, H., Fujimura, T., Murayama, K., Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine (1998) J. Biol. Chem., 273, pp. 14085-14089
• Quijano, C., Hernandez-Saavedra, D., Castro, L., McCord, J.M., Freeman, B., Radi, R., Reaction of peroxynitrite with mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration (2001) J. Biol. Chem., 276, pp. 11631-11638
• Surmeli, N.B., Litterman, N.K., Miller, A.F., Groves, J.T., Peroxynitrite mediates active site tyrosine nitration in manganese superoxide dismutase: Evidence of a role for the carbonate radical anion (2010) J. Am. Chem. Soc., 132, pp. 17174-17185
• Moreno, D.M., Martí, M.A., De Biase, P.M., Estrin, D.A., Demicheli, V., Radi, R., Boechi, L., Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration (2011) Arch. Biochem. Biophys., 507, pp. 304-309
• Radi, R., Protein tyrosine nitration: Biochemical mechanisms and structural basis of functional effects (2013) Acc. Chem. Res., 46, pp. 550-559
• Radi, R., Beckman, J.S., Bush, K.M., Freeman, B., Peroxynitrite- induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide (1991) Arch. Biochem. Biophys., 288, pp. 481-487
• Hughes, M.N., Nicklin, H.G., A possible role for the species peroxonitrite in nitrification (1970) Biochim. Biophys. Acta, 222, pp. 660-661
• Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
• Crow, J.P., Sampson, J.B., Zhuang, Y., Thompson, J.A., Beckman, J.S., Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite (1997) J. Neurochem., 69, pp. 1936-1944
• McCord, J.M., Fridovich, I., Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein (1969) J. Biol. Chem., 244, pp. 6049-6055
• Peskin, A.V., Winterbourn, C.C., Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3- phosphate dehydrogenase (2006) Free Radic. Biol. Med., 40, pp. 45-53
• Alvarez, B., Ferrer-Sueta, G., Freeman, B., Radi, R., Kinetics of peroxynitrite reaction with amino acids and human serum albumin (1999) J. Biol. Chem., 274, pp. 842-848
• Ellman, G.L., Tissue sulfhydryl groups (1959) Arch. Biochem. Biophys., 82, pp. 70-77
• Trujillo, M., Budde, H., Pineyro, M.D., Stehr, M., Robello, C., Flohé, L., Radi, R., Trypanosoma brucei and trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols (2004) J. Biol. Chem., 279, pp. 34175-34182
• Brito, C., Naviliat, M., Tiscornia, A.C., Vuillier, F., Gualco, G., Dighiero, G., Radi, R., Cayota, A.M., Peroxynitrite inhibits t lymphocyte activation and proliferation by promoting impairment of tyrosine phosphorylation and peroxynitrite-driven apoptotic death (1999) J. Immunol., 162, pp. 3356-3366
• Peloso, E.F., Gonçalves, C.C., Silva, T.M., Ribeiro, L.H., Pineyro, M.D., Robello, C., Gadelha, F.R., Tryparedoxin peroxidases and superoxide dismutases expression as well as ros release are related to trypanosoma cruzi epimastigotes growth phases (2012) Arch. Biochem. Biophys., 520, pp. 117-122
• Romero, N., Radi, R., Linares, E., Augusto, O., Detweiler, C.D., Mason, R.P., Denicola, A., Reaction of human hemoglobin with peroxynitrite: Isomerization to nitrate and secondary formation of protein radicals (2003) J. Biol. Chem., 278, pp. 44049-44057
• Hellman, U., Sample preparation by sds/page and in-gel digestion (2000) EXS, 88, pp. 43-54
• Nicholls, S.J., Shen, Z., Fu, X., Levison, B.S., Hazen, S.L., Quantification of 3-nitrotyrosine levels using a benchtop ion trap mass spectrometry method (2005) Methods Enzymol., 396, pp. 245-266
• Turko, I.V., Murad, F., Mapping sites of tyrosine nitration by matrix-assisted laser desorption/ionization mass spectrometry (2005) Methods Enzymol., 396, pp. 266-275
• Leslie, A.G.W., Processing difraction data with mosflm (2007) Evolving Methods for Macromolecular Crystallography, pp. 41-51. , (Read, R. J., and Sussman, J. L., eds) Springer, New York
• Evans, P., Scaling and assessment of data quality (2006) Acta Crystallogr.D Biol. Crystallogr., 62, pp. 72-82
• Trapani, S., Navaza, J., Amore: Classical and modern (2008) Acta Crystallogr. D Biol. Crystallogr., 64, pp. 11-16
• Vonrhein, C., Flensburg, C., Keller, P., Sharff, A., Smart, O., Paciorek, W., Womack, T., Bricogne, G., Data processing and analysis with the autoproc toolbox (2011) Acta Crystallogr. D Biol. Crystallogr., 67, pp. 293-302
• Emsley, P., Lohkamp, B., Scott, W.G., Cowtan, K., Features and development of coot (2010) Acta Crystallogr. D Biol. Crystallogr., 66, pp. 486-501
• Chen, V.B., Arendall III, W.B., Headd, J.J., Keedy, D.A., Immormino, R.M., Kapral, G.J., Murray, L.W., Richardson, D.C., Molprobity: All-atom structure validation for macromolecular crystallography (2010) Acta Crystallogr. D Biol. Crystallogr., 66, pp. 12-21
• Cheatham III, T.E., Cieplak, P., Kollman, P.A., A modified version of the cornell et al. Force field with improved sugar pucker phases and helical repeat (1999) J. Biomol. Struct. Dyn., 16, pp. 845-862
• Petruk, A.A., Bartesaghi, S., Trujillo, M., Estrin, D.A., Murgida, D., Kalyanaraman, B., Marti, M.A., Radi, R., Molecular basis of intramolecular electron transfer in proteins during radical-mediated oxidations: Computer simulation studies in model tyrosine-cysteine peptides in solution (2012) Arch. Biochem. Biophys., 525, pp. 82-91
• Leach, A., (2001) Molecular Modelling: Principles and Applications, , Prentice Hall, New York
• Case, D., Darden, T., Cheatham, T., Simmerling, C., Wang, J., Duke, R., Luo, R., Kollman, P.A., (2006) AMBER, 9. , University of California, San Francisco, California
• Beratan, D.N., Betts, J.N., Onuchic, J.N., Protein electron transfer rates set by the bridging secondary and tertiary structure (1991) Science, 252, pp. 1285-1288
• Beratan, D.N., Onuchic, J.N., Winkler, J.R., Gray, H.B., Electron- tunneling pathways in proteins (1992) Science, 258, pp. 1740-1741
• Shih, C., Museth, A.K., Abrahamsson, M., Blanco-Rodriguez, A.M., Di Bilio, A.J., Sudhamsu, J., Crane, B.R., Gray, H.B., Tryptophanaccelerated electron flow through proteins (2008) Science, 320, pp. 1760-1762
• Stubbe, J., Nocera, D.G., Yee, C.S., Chang, M.C., Radical initiation in the class i ribonucleotide reductase: Long-range proton-coupled electron transfer? (2003) Chem. Rev., 103, pp. 2167-2201
• Alvarez-Paggi, D., Martín, D.F., DeBiase, P.M., Hildebrandt, P., Martí, M.A., Murgida, D.H., Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes (2010) J. Am. Chem. Soc., 132, pp. 5769-5778
• Aubert, C., Mathis, P., Eker, A.P., Brettel, K., Intraprotein electron transfer between tyrosine and tryptophan in dna photolyase from anacystis nidulans (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 5423-5427
• Ly, H.K., Marti, M.A., Martin, D.F., Alvarez-Paggi, D., Meister, W., Kranich, A., Weidinger, I.M., Murgida, D.H., Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes (2010) Chemphyschem, 11, pp. 1225-1235
• Li, H., Robertson, A.D., Jensen, J.H., Very fast empirical prediction and rationalization of protein pka values (2005) Proteins, 61, pp. 704-721
• Bas, D.C., Rogers, D.M., Jensen, J.H., Very fast prediction and rationalization of pka values for protein-ligand complexes (2008) Proteins, 73, pp. 765-783
• Olsson, M.H.M., Sondergaard, C.R., Rostkowski, M., Jensen, J.H., Propka3: Consistent treatment of internal and surface residues in empirical pka predictions (2011) J. Chem. Theory Comput., 7, pp. 525-537
• Sondergaard, C.R., Olsson, M.H.M., Rostkowski, M., Jensen, J.H., Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pka values (2011) J. Chem. Theory Comput., 7, pp. 2284-2295
• Taylor, M.C., Kelly, J.M., Ptcindex: A stable tetracyclineregulated expression vector for trypanosoma cruzi (2006) BMCBiotechnol., 6, p. 32
• Piacenza, L., Peluffo, G., Alvarez, M.N., Kelly, J.M., Wilkinson, S.R., Radi, R., Peroxiredoxins play a major role in protecting trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite (2008) Biochem. J., 410, pp. 359-368
• Wilkinson, S.R., Prathalingam, S.R., Taylor, M.C., Ahmed, A., Horn, D., Kelly, J.M., Functional characterisation of the iron superoxide dismutase gene repertoire in trypanosoma brucei (2006) Free Radic. Biol. Med., 40, pp. 198-209
• Forman, H.J., Fridovich, I., Superoxide dismutase: A comparison of rate constants (1973) Arch. Biochem. Biophys., 158, pp. 396-400
• Crow, J.P., Beckman, J.S., McCord, J.M., Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite (1995) Biochemistry, 34, pp. 3544-3552
• Zou, M.H., Daiber, A., Peterson, J.A., Shoun, H., Ullrich, V., Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration (2000) Arch. Biochem. Biophys., 376, pp. 149-155
• Ferrer-Sueta, G., Radi, R., Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals (2009) ACS Chem. Biol., 4, pp. 161-177
• Radi, R., Nitric oxide, oxidants, and protein tyrosine nitration (2004) Proc. Natl. Acad. Sci. U.S.A., 101, pp. 4003-4008
• Tien, M., Berlett, B.S., Levine, R.L., Chock, P.B., Stadtman, E.R., Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concentration: Ph dependence of carbonyl formation, tyrosine nitration, and methionine oxidation (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 7809-7814
• Denicola, A., Freeman, B., Trujillo, M., Radi, R., Peroxynitrite reaction with carbon dioxide/bicarbonate: Kinetics and influence on peroxynitrite- mediated oxidations (1996) Arch. Biochem. Biophys., 333, pp. 49-58
• Lymar, S.V., Hurst, J.K., Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant? (1996) Chem. Res. Toxicol., 9, pp. 845-850
• Pryor, W.A., Lemercier, J.N., Zhang, H., Uppu, R.M., Squadrito, G.L., The catalytic role of carbon dioxide in the decomposition of peroxynitrite (1997) Free Radic. Biol. Med., 23, pp. 331-338
• Koppenol, W.H., Kissner, R., Can onooh undergo homolysis? (1998) Chem. Res. Toxicol., 11, pp. 87-90
• Koppenol, W.H., Moreno, J.J., Pryor, W.A., Ischiropoulos, H., Beckman, J.S., Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide (1992) Chem. Res. Toxicol., 5, pp. 834-842
• Ford, E., Hughes, M.N., Wardman, P., Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological ph (2002) Free Radic. Biol. Med., 32, pp. 1314-1323
• Reiter, C.D., Teng, R.J., Beckman, J.S., Superoxide reacts with nitric oxide to nitrate tyrosine at physiological ph via peroxynitrite (2000) J. Biol. Chem., 275, pp. 32460-32466
• Sawa, T., Akaike, T., Maeda, H., Tyrosine nitration by peroxynitrite formed from nitric oxide and superoxide generated by xanthine oxidase (2000) J. Biol. Chem., 275, pp. 32467-32474
• Abriata, L.A., Cassina, A., Tórtora, V., Marín, M., Souza, J.M., Castro, L., Vila, A.J., Radi, R., Nitration of solvent-exposed tyrosine 74 on cytochrome c triggers heme iron-methionine 80 bond disruption: Nuclear magnetic resonance and optical spectroscopy studies (2009) J. Biol. Chem., 284, pp. 17-26
• Bachega, J.F., Navarro, M.V., Bleicher, L., Bortoleto-Bugs, R.K., Dive, D., Hoffmann, P., Viscogliosi, E., Garratt, R.C., Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity (2009) Proteins, 77, pp. 26-37
• Boucher, I.W., Brzozowski, A.M., Brannigan, J.A., Schnick, C., Smith, D.J., Kyes, S.A., Wilkinson, A.J., The crystal structure of superoxide dismutase from plasmodium falciparum (2006) BMC Struct. Biol., 6, p. 20
• Guan, Y., Hickey, M.J., Borgstahl, G.E., Hallewell, R.A., Lepock, J.R., O'Connor, D., Hsieh, Y., Tainer, J.A., Crystal structure of y34f mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34 (1998) Biochemistry, 37, pp. 4722-4730
• Reece, S.Y., Hodgkiss, J.M., Stubbe, J., Nocera, D.G., Protoncoupled electron transfer: The mechanistic underpinning for radical transport and catalysis in biology (2006) Philos. Trans. R. Soc. Lond B Biol. Sci., 361, pp. 1351-1364
• Bhattacharjee, S., Deterding, L.J., Jiang, J., Bonini, M.G., Tomer, K.B., Ramirez, D.C., Mason, R.P., Electron transfer between a tyrosyl radical and a cysteine residue in hemoproteins: Spin trapping analysis (2007) J. Am. Chem. Soc., 129, pp. 13493-13501
• Witting, P.K., Mauk, A.G., Reaction of human myoglobin and h2o2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical (2001) J. Biol. Chem., 276, pp. 16540-16547
• Giese, B., Graber, M., Cordes, M., Electron transfer in peptides and proteins (2008) Curr. Opin. Chem. Biol., 12, pp. 755-759
• Cordes, M., Köttgen, A., Jasper, C., Jacques, O., Boudebous, H., Giese, B., Influence of amino acid side chains on long-distance electron transfer in peptides: Electron hopping via "stepping stones" (2008) Angew Chem. Int. Ed. Engl., 47, pp. 3461-3463
• Graceffa, P., Spin labeling of protein sulfhydryl groups by spin trapping a sulfur radical: Application to bovine serum albumin and myosin (1983) Arch. Biochem. Biophys., 225, pp. 802-808
• Maples, K.R., Jordan, S.J., Mason, R.P., In vivo rat hemoglobin thiyl free radical formation following administration of phenylhydrazine and hydrazine-based drugs (1988) Drug Metab. Dispos., 16, pp. 799-803
• Gatti, R.M., Radi, R., Augusto, O., Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical (1994) FEBS Lett., 348, pp. 287-290
• Carballal, S., Bartesaghi, S., Radi, R., Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite (2014) Biochim. Biophys. Acta, 1840, pp. 768-780
• Fasman, G.D., (1976) Handbook of Biochemistry and Molecular Biology: Physical Data and Chemical Data, pp. 305-351. , CRC Press, Inc., Cleveland, OH
• Radi, R., Peroxynitrite, a stealthy biological oxidant (2013) J. Biol. Chem., 288, pp. 26464-26472
• Quint, P., Reutzel, R., Mikulski, R., McKenna, R., Silverman, D.N., Crystal structure of nitrated human manganese superoxide dismutase: Mechanism of inactivation (2006) Free Radic. Biol. Med., 40, pp. 453-458
• Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J.C., Smith, C.D., Beckman, J.S., Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase (1992) Arch. Biochem. Biophys., 298, pp. 431-437
• Adams, P.D., Afonine, P.V., Bunkóczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Zwart, P.H., Phenix: A comprehensive python-based system for macromolecular structure solution (2010) Acta Crystallogr. D Biol. Crystallogr., 66, pp. 213-221

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