Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilitie...

Autores: Martinez, Alejandra; Peluffo, Gonzalo; Petruk, Ariel Alcides; Hugo, Martín; Piñeyro, Dolores; Demicheli, Veronica; Moreno, Diego Martin; Lima, Analia Ethel; Batthyány, Carlos; Duran, Rosario; Robledo, Carlos Walter; Marti, Marcelo Adrian; Larrieux, Nicole; Buschiazzo, Alejandro; Trujillo, Madia; Radi, Rafael; Piacenza, Lucia
Año de publicación: 2014
Idioma: inglés
Tipo de recurso: artículo
Estado: versión publicada
Descripción: Trypanosoma cruzi, the causative agent of Chagas disease, contains exclusively iron-dependent superoxide dismutases (Fe-SODs) located in different subcellular compartments. Peroxynitrite, a key cytotoxic and oxidizing effector biomolecule, reacted with T. cruzi mitochondrial (Fe-SODA) and cytosolic (Fe-SODB) SODs with second order rate constants of 4.6 ± 0.2 × 104 M−1 s−1 and 4.3 ± 0.4 × 104 M−1 s−1 at pH 7.4 and 37 °C, respectively. Both isoforms are dose-dependently nitrated and inactivated by peroxynitrite. Susceptibility of T. cruzi Fe-SODA toward peroxynitrite was similar to that reported previously for Escherichia coli Mn- and Fe-SODs and mammalian Mn-SOD, whereas Fe-SODB was exceptionally resistant to oxidant-mediated inactivation. We report mass spectrometry analysis indicating that peroxynitrite-mediated inactivation of T. cruzi Fe-SODs is due to the site-specific nitration of the critical and universally conserved Tyr35. Searching for structural differences, the crystal structure of Fe-SODA was solved at 2.2 Å resolution. Structural analysis comparing both Fe-SOD isoforms reveals differences in key cysteines and tryptophan residues. Thiol alkylation of Fe-SODB cysteines made the enzyme more susceptible to peroxynitrite. In particular, Cys83 mutation (C83S, absent in Fe-SODA) increased the Fe-SODB sensitivity toward peroxynitrite. Molecular dynamics, electron paramagnetic resonance, and immunospin trapping analysis revealed that Cys83 present in Fe-SODB acts as an electron donor that repairs Tyr35 radical via intramolecular electron transfer, preventing peroxynitrite-dependent nitration and consequent inactivation of Fe-SODB. Parasites exposed to exogenous or endogenous sources of peroxynitrite resulted in nitration and inactivation of Fe-SODA but not Fe-SODB, suggesting that these enzymes play distinctive biological roles during parasite infection of mammalian cells.
Fil: Martinez, Alejandra. Universidad de la República; Uruguay
Fil: Peluffo, Gonzalo. Universidad de la República; Uruguay
Fil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad Nacional de Tucumán; Argentina
Fil: Hugo, Martín. Universidad de la República; Uruguay
Fil: Piñeyro, Dolores. Universidad de la República; Uruguay
Fil: Demicheli, Veronica. Universidad de la República; Uruguay
Fil: Moreno, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina
Fil: Lima, Analia Ethel. Instituto Pasteur de Montevideo; Uruguay
Fil: Batthyány, Carlos. Instituto Pasteur de Montevideo; Uruguay. Universidad de la República; Uruguay
Fil: Duran, Rosario. Instituto Pasteur de Montevideo; Uruguay
Fil: Robledo, Carlos Walter. Universidad de la República; Uruguay
Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Larrieux, Nicole. Instituto Pasteur de Montevideo; Uruguay
Fil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; Francia
Fil: Trujillo, Madia. Universidad de la República; Uruguay
Fil: Radi, Rafael. Universidad de la República; Uruguay
Fil: Piacenza, Lucia. Universidad de la República; Uruguay
Materia: Free Radicals
Nitric Oxide
Oxidation-Reduction
Superoxide Dismutase (Sod)
Trypanosome
Trypanosoma Cruzi
Nitration
Peroxynitrite
Superoxide
Nivel de accesibilidad: acceso abierto
Condiciones de uso: https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
Institución: Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador: oai:ri.conicet.gov.ar:11336/31213

Acceder

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network_acronym_str	CONICETDig
repository_id_str	3498
network_name_str	CONICET Digital (CONICET)
spelling	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transferMartinez, AlejandraPeluffo, GonzaloPetruk, Ariel AlcidesHugo, MartínPiñeyro, DoloresDemicheli, VeronicaMoreno, Diego MartinLima, Analia EthelBatthyány, CarlosDuran, RosarioRobledo, Carlos WalterMarti, Marcelo AdrianLarrieux, NicoleBuschiazzo, AlejandroTrujillo, MadiaRadi, RafaelPiacenza, LuciaFree RadicalsNitric OxideOxidation-ReductionSuperoxide Dismutase (Sod)TrypanosomeTrypanosoma CruziNitrationPeroxynitriteSuperoxidehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Trypanosoma cruzi, the causative agent of Chagas disease, contains exclusively iron-dependent superoxide dismutases (Fe-SODs) located in different subcellular compartments. Peroxynitrite, a key cytotoxic and oxidizing effector biomolecule, reacted with T. cruzi mitochondrial (Fe-SODA) and cytosolic (Fe-SODB) SODs with second order rate constants of 4.6 ± 0.2 × 104 M−1 s−1 and 4.3 ± 0.4 × 104 M−1 s−1 at pH 7.4 and 37 °C, respectively. Both isoforms are dose-dependently nitrated and inactivated by peroxynitrite. Susceptibility of T. cruzi Fe-SODA toward peroxynitrite was similar to that reported previously for Escherichia coli Mn- and Fe-SODs and mammalian Mn-SOD, whereas Fe-SODB was exceptionally resistant to oxidant-mediated inactivation. We report mass spectrometry analysis indicating that peroxynitrite-mediated inactivation of T. cruzi Fe-SODs is due to the site-specific nitration of the critical and universally conserved Tyr35. Searching for structural differences, the crystal structure of Fe-SODA was solved at 2.2 Å resolution. Structural analysis comparing both Fe-SOD isoforms reveals differences in key cysteines and tryptophan residues. Thiol alkylation of Fe-SODB cysteines made the enzyme more susceptible to peroxynitrite. In particular, Cys83 mutation (C83S, absent in Fe-SODA) increased the Fe-SODB sensitivity toward peroxynitrite. Molecular dynamics, electron paramagnetic resonance, and immunospin trapping analysis revealed that Cys83 present in Fe-SODB acts as an electron donor that repairs Tyr35 radical via intramolecular electron transfer, preventing peroxynitrite-dependent nitration and consequent inactivation of Fe-SODB. Parasites exposed to exogenous or endogenous sources of peroxynitrite resulted in nitration and inactivation of Fe-SODA but not Fe-SODB, suggesting that these enzymes play distinctive biological roles during parasite infection of mammalian cells.Fil: Martinez, Alejandra. Universidad de la República; UruguayFil: Peluffo, Gonzalo. Universidad de la República; UruguayFil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad Nacional de Tucumán; ArgentinaFil: Hugo, Martín. Universidad de la República; UruguayFil: Piñeyro, Dolores. Universidad de la República; UruguayFil: Demicheli, Veronica. Universidad de la República; UruguayFil: Moreno, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; ArgentinaFil: Lima, Analia Ethel. Instituto Pasteur de Montevideo; UruguayFil: Batthyány, Carlos. Instituto Pasteur de Montevideo; Uruguay. Universidad de la República; UruguayFil: Duran, Rosario. Instituto Pasteur de Montevideo; UruguayFil: Robledo, Carlos Walter. Universidad de la República; UruguayFil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Larrieux, Nicole. Instituto Pasteur de Montevideo; UruguayFil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; FranciaFil: Trujillo, Madia. Universidad de la República; UruguayFil: Radi, Rafael. Universidad de la República; UruguayFil: Piacenza, Lucia. Universidad de la República; UruguayAmerican Society for Biochemistry and Molecular Biology2014-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31213Martinez, Alejandra; Peluffo, Gonzalo; Petruk, Ariel Alcides; Hugo, Martín; Piñeyro, Dolores; et al.; Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 5-2014; 12760-127780021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M113.545590info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/289/18/12760info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:59:03Zoai:ri.conicet.gov.ar:11336/31213instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:59:03.315CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
title	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
spellingShingle	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer Martinez, Alejandra Free Radicals Nitric Oxide Oxidation-Reduction Superoxide Dismutase (Sod) Trypanosome Trypanosoma Cruzi Nitration Peroxynitrite Superoxide
title_short	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
title_full	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
title_fullStr	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
title_full_unstemmed	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
title_sort	Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
dc.creator.none.fl_str_mv	Martinez, Alejandra Peluffo, Gonzalo Petruk, Ariel Alcides Hugo, Martín Piñeyro, Dolores Demicheli, Veronica Moreno, Diego Martin Lima, Analia Ethel Batthyány, Carlos Duran, Rosario Robledo, Carlos Walter Marti, Marcelo Adrian Larrieux, Nicole Buschiazzo, Alejandro Trujillo, Madia Radi, Rafael Piacenza, Lucia
author	Martinez, Alejandra
author_facet	Martinez, Alejandra Peluffo, Gonzalo Petruk, Ariel Alcides Hugo, Martín Piñeyro, Dolores Demicheli, Veronica Moreno, Diego Martin Lima, Analia Ethel Batthyány, Carlos Duran, Rosario Robledo, Carlos Walter Marti, Marcelo Adrian Larrieux, Nicole Buschiazzo, Alejandro Trujillo, Madia Radi, Rafael Piacenza, Lucia
author_role	author
author2	Peluffo, Gonzalo Petruk, Ariel Alcides Hugo, Martín Piñeyro, Dolores Demicheli, Veronica Moreno, Diego Martin Lima, Analia Ethel Batthyány, Carlos Duran, Rosario Robledo, Carlos Walter Marti, Marcelo Adrian Larrieux, Nicole Buschiazzo, Alejandro Trujillo, Madia Radi, Rafael Piacenza, Lucia
author2_role	author author author author author author author author author author author author author author author author
dc.subject.none.fl_str_mv	Free Radicals Nitric Oxide Oxidation-Reduction Superoxide Dismutase (Sod) Trypanosome Trypanosoma Cruzi Nitration Peroxynitrite Superoxide
topic	Free Radicals Nitric Oxide Oxidation-Reduction Superoxide Dismutase (Sod) Trypanosome Trypanosoma Cruzi Nitration Peroxynitrite Superoxide
purl_subject.fl_str_mv	https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv	Trypanosoma cruzi, the causative agent of Chagas disease, contains exclusively iron-dependent superoxide dismutases (Fe-SODs) located in different subcellular compartments. Peroxynitrite, a key cytotoxic and oxidizing effector biomolecule, reacted with T. cruzi mitochondrial (Fe-SODA) and cytosolic (Fe-SODB) SODs with second order rate constants of 4.6 ± 0.2 × 104 M−1 s−1 and 4.3 ± 0.4 × 104 M−1 s−1 at pH 7.4 and 37 °C, respectively. Both isoforms are dose-dependently nitrated and inactivated by peroxynitrite. Susceptibility of T. cruzi Fe-SODA toward peroxynitrite was similar to that reported previously for Escherichia coli Mn- and Fe-SODs and mammalian Mn-SOD, whereas Fe-SODB was exceptionally resistant to oxidant-mediated inactivation. We report mass spectrometry analysis indicating that peroxynitrite-mediated inactivation of T. cruzi Fe-SODs is due to the site-specific nitration of the critical and universally conserved Tyr35. Searching for structural differences, the crystal structure of Fe-SODA was solved at 2.2 Å resolution. Structural analysis comparing both Fe-SOD isoforms reveals differences in key cysteines and tryptophan residues. Thiol alkylation of Fe-SODB cysteines made the enzyme more susceptible to peroxynitrite. In particular, Cys83 mutation (C83S, absent in Fe-SODA) increased the Fe-SODB sensitivity toward peroxynitrite. Molecular dynamics, electron paramagnetic resonance, and immunospin trapping analysis revealed that Cys83 present in Fe-SODB acts as an electron donor that repairs Tyr35 radical via intramolecular electron transfer, preventing peroxynitrite-dependent nitration and consequent inactivation of Fe-SODB. Parasites exposed to exogenous or endogenous sources of peroxynitrite resulted in nitration and inactivation of Fe-SODA but not Fe-SODB, suggesting that these enzymes play distinctive biological roles during parasite infection of mammalian cells. Fil: Martinez, Alejandra. Universidad de la República; Uruguay Fil: Peluffo, Gonzalo. Universidad de la República; Uruguay Fil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad Nacional de Tucumán; Argentina Fil: Hugo, Martín. Universidad de la República; Uruguay Fil: Piñeyro, Dolores. Universidad de la República; Uruguay Fil: Demicheli, Veronica. Universidad de la República; Uruguay Fil: Moreno, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina Fil: Lima, Analia Ethel. Instituto Pasteur de Montevideo; Uruguay Fil: Batthyány, Carlos. Instituto Pasteur de Montevideo; Uruguay. Universidad de la República; Uruguay Fil: Duran, Rosario. Instituto Pasteur de Montevideo; Uruguay Fil: Robledo, Carlos Walter. Universidad de la República; Uruguay Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Larrieux, Nicole. Instituto Pasteur de Montevideo; Uruguay Fil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; Francia Fil: Trujillo, Madia. Universidad de la República; Uruguay Fil: Radi, Rafael. Universidad de la República; Uruguay Fil: Piacenza, Lucia. Universidad de la República; Uruguay
description	Trypanosoma cruzi, the causative agent of Chagas disease, contains exclusively iron-dependent superoxide dismutases (Fe-SODs) located in different subcellular compartments. Peroxynitrite, a key cytotoxic and oxidizing effector biomolecule, reacted with T. cruzi mitochondrial (Fe-SODA) and cytosolic (Fe-SODB) SODs with second order rate constants of 4.6 ± 0.2 × 104 M−1 s−1 and 4.3 ± 0.4 × 104 M−1 s−1 at pH 7.4 and 37 °C, respectively. Both isoforms are dose-dependently nitrated and inactivated by peroxynitrite. Susceptibility of T. cruzi Fe-SODA toward peroxynitrite was similar to that reported previously for Escherichia coli Mn- and Fe-SODs and mammalian Mn-SOD, whereas Fe-SODB was exceptionally resistant to oxidant-mediated inactivation. We report mass spectrometry analysis indicating that peroxynitrite-mediated inactivation of T. cruzi Fe-SODs is due to the site-specific nitration of the critical and universally conserved Tyr35. Searching for structural differences, the crystal structure of Fe-SODA was solved at 2.2 Å resolution. Structural analysis comparing both Fe-SOD isoforms reveals differences in key cysteines and tryptophan residues. Thiol alkylation of Fe-SODB cysteines made the enzyme more susceptible to peroxynitrite. In particular, Cys83 mutation (C83S, absent in Fe-SODA) increased the Fe-SODB sensitivity toward peroxynitrite. Molecular dynamics, electron paramagnetic resonance, and immunospin trapping analysis revealed that Cys83 present in Fe-SODB acts as an electron donor that repairs Tyr35 radical via intramolecular electron transfer, preventing peroxynitrite-dependent nitration and consequent inactivation of Fe-SODB. Parasites exposed to exogenous or endogenous sources of peroxynitrite resulted in nitration and inactivation of Fe-SODA but not Fe-SODB, suggesting that these enzymes play distinctive biological roles during parasite infection of mammalian cells.
publishDate	2014
dc.date.none.fl_str_mv	2014-05
dc.type.none.fl_str_mv	info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo
format	article
status_str	publishedVersion
dc.identifier.none.fl_str_mv	http://hdl.handle.net/11336/31213 Martinez, Alejandra; Peluffo, Gonzalo; Petruk, Ariel Alcides; Hugo, Martín; Piñeyro, Dolores; et al.; Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 5-2014; 12760-12778 0021-9258 CONICET Digital CONICET
url	http://hdl.handle.net/11336/31213
identifier_str_mv	Martinez, Alejandra; Peluffo, Gonzalo; Petruk, Ariel Alcides; Hugo, Martín; Piñeyro, Dolores; et al.; Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 5-2014; 12760-12778 0021-9258 CONICET Digital CONICET
dc.language.none.fl_str_mv	eng
language	eng
dc.relation.none.fl_str_mv	info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M113.545590 info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/289/18/12760
dc.rights.none.fl_str_mv	info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv	openAccess
rights_invalid_str_mv	https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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dc.publisher.none.fl_str_mv	American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv	American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv	reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas
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repository.name.fl_str_mv	CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv	dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score	13.070432

Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma Cruzi iron-superoxide dismutases (fe-sods) A and B. Disparate susceptibilitie...

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