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

Background: Superoxide dismutases are inactivated by peroxynitrite. Results: T. cruzi cytosolic Fe-SODB is highly resistant toward peroxynitrite-mediated tyrosine nitration and inactivation as compared with mitochondrial Fe-SODA. Conclusion: Intramolecular electron transfer in Fe-SODB from Cys83 to...

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Autores principales:	Petruk, Ariel Alcides, Martí, Marcelo Adrián, Buschiazzo, Alejandro
Publicado:	2014
Materias:	Amino acids Electron transitions Nitration Oxygen Repair Cytosolic Intra-molecular electron transfer Mammalian cells Molecular basis Peroxynitrites Superoxide dismutases Trypanosoma cruzi Tyrosine nitration Free radical reactions cysteine iron superoxide dismutase isoenzyme mitochondrial enzyme peroxynitrite tryptophan tyrosine alkylation article controlled study crystal structure cytosol electron transport enzyme active site enzyme analysis enzyme inactivation enzyme structure mass spectrometry molecular biology mutation nitration nonhuman priority journal structure analysis Free Radicals Nitric Oxide Oxidation-Reduction Peroxynitrite Superoxide Superoxide Dismutase (SOD) Trypanosome Animals Binding Sites Blotting, Western Catalytic Domain Chagas Disease Crystallography, X-Ray Cysteine Electron Spin Resonance Spectroscopy Electron Transport Enzyme Activation Host-Parasite Interactions Isoenzymes Kinetics Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Nitrates Peroxynitrous Acid Protein Binding Protein Structure, Secondary Protozoan Proteins Reactive Oxygen Species Superoxide Dismutase Tyrosine
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v289_n18_p12760_Martinez http://hdl.handle.net/20.500.12110/paper_00219258_v289_n18_p12760_Martinez
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00219258_v289_n18_p12760_Martinez
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spelling	paper:paper_00219258_v289_n18_p12760_Martinez2023-06-08T14:43:36Z 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 Petruk, Ariel Alcides Martí, Marcelo Adrián Buschiazzo, Alejandro Amino acids Electron transitions Nitration Oxygen Repair Cytosolic Intra-molecular electron transfer Mammalian cells Molecular basis Peroxynitrites Superoxide dismutases Trypanosoma cruzi Tyrosine nitration Free radical reactions cysteine iron superoxide dismutase isoenzyme mitochondrial enzyme peroxynitrite tryptophan tyrosine alkylation article controlled study crystal structure cytosol electron transport enzyme active site enzyme analysis enzyme inactivation enzyme structure mass spectrometry molecular biology mutation nitration nonhuman priority journal structure analysis Trypanosoma cruzi Free Radicals Nitration Nitric Oxide Oxidation-Reduction Peroxynitrite Superoxide Superoxide Dismutase (SOD) Trypanosoma cruzi Trypanosome Animals Binding Sites Blotting, Western Catalytic Domain Chagas Disease Crystallography, X-Ray Cysteine Electron Spin Resonance Spectroscopy Electron Transport Enzyme Activation Host-Parasite Interactions Isoenzymes Kinetics Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Nitrates Peroxynitrous Acid Protein Binding Protein Structure, Secondary Protozoan Proteins Reactive Oxygen Species Superoxide Dismutase Trypanosoma cruzi Tyrosine Background: Superoxide dismutases are inactivated by peroxynitrite. Results: T. cruzi cytosolic Fe-SODB is highly resistant toward peroxynitrite-mediated tyrosine nitration and inactivation as compared with mitochondrial Fe-SODA. Conclusion: Intramolecular electron transfer in Fe-SODB from Cys83 to critical Tyr35 prevents enzyme nitration and inactivation. Significance: Disparate susceptibilities of Fe-SODs to peroxynitrite can influence parasite virulence during T. cruzi infection of mammalian cells. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Fil:Petruk, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Buschiazzo, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v289_n18_p12760_Martinez http://hdl.handle.net/20.500.12110/paper_00219258_v289_n18_p12760_Martinez
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Amino acids Electron transitions Nitration Oxygen Repair Cytosolic Intra-molecular electron transfer Mammalian cells Molecular basis Peroxynitrites Superoxide dismutases Trypanosoma cruzi Tyrosine nitration Free radical reactions cysteine iron superoxide dismutase isoenzyme mitochondrial enzyme peroxynitrite tryptophan tyrosine alkylation article controlled study crystal structure cytosol electron transport enzyme active site enzyme analysis enzyme inactivation enzyme structure mass spectrometry molecular biology mutation nitration nonhuman priority journal structure analysis Trypanosoma cruzi Free Radicals Nitration Nitric Oxide Oxidation-Reduction Peroxynitrite Superoxide Superoxide Dismutase (SOD) Trypanosoma cruzi Trypanosome Animals Binding Sites Blotting, Western Catalytic Domain Chagas Disease Crystallography, X-Ray Cysteine Electron Spin Resonance Spectroscopy Electron Transport Enzyme Activation Host-Parasite Interactions Isoenzymes Kinetics Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Nitrates Peroxynitrous Acid Protein Binding Protein Structure, Secondary Protozoan Proteins Reactive Oxygen Species Superoxide Dismutase Trypanosoma cruzi Tyrosine
spellingShingle	Amino acids Electron transitions Nitration Oxygen Repair Cytosolic Intra-molecular electron transfer Mammalian cells Molecular basis Peroxynitrites Superoxide dismutases Trypanosoma cruzi Tyrosine nitration Free radical reactions cysteine iron superoxide dismutase isoenzyme mitochondrial enzyme peroxynitrite tryptophan tyrosine alkylation article controlled study crystal structure cytosol electron transport enzyme active site enzyme analysis enzyme inactivation enzyme structure mass spectrometry molecular biology mutation nitration nonhuman priority journal structure analysis Trypanosoma cruzi Free Radicals Nitration Nitric Oxide Oxidation-Reduction Peroxynitrite Superoxide Superoxide Dismutase (SOD) Trypanosoma cruzi Trypanosome Animals Binding Sites Blotting, Western Catalytic Domain Chagas Disease Crystallography, X-Ray Cysteine Electron Spin Resonance Spectroscopy Electron Transport Enzyme Activation Host-Parasite Interactions Isoenzymes Kinetics Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Nitrates Peroxynitrous Acid Protein Binding Protein Structure, Secondary Protozoan Proteins Reactive Oxygen Species Superoxide Dismutase Trypanosoma cruzi Tyrosine Petruk, Ariel Alcides Martí, Marcelo Adrián Buschiazzo, Alejandro 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
topic_facet	Amino acids Electron transitions Nitration Oxygen Repair Cytosolic Intra-molecular electron transfer Mammalian cells Molecular basis Peroxynitrites Superoxide dismutases Trypanosoma cruzi Tyrosine nitration Free radical reactions cysteine iron superoxide dismutase isoenzyme mitochondrial enzyme peroxynitrite tryptophan tyrosine alkylation article controlled study crystal structure cytosol electron transport enzyme active site enzyme analysis enzyme inactivation enzyme structure mass spectrometry molecular biology mutation nitration nonhuman priority journal structure analysis Trypanosoma cruzi Free Radicals Nitration Nitric Oxide Oxidation-Reduction Peroxynitrite Superoxide Superoxide Dismutase (SOD) Trypanosoma cruzi Trypanosome Animals Binding Sites Blotting, Western Catalytic Domain Chagas Disease Crystallography, X-Ray Cysteine Electron Spin Resonance Spectroscopy Electron Transport Enzyme Activation Host-Parasite Interactions Isoenzymes Kinetics Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Nitrates Peroxynitrous Acid Protein Binding Protein Structure, Secondary Protozoan Proteins Reactive Oxygen Species Superoxide Dismutase Trypanosoma cruzi Tyrosine
description	Background: Superoxide dismutases are inactivated by peroxynitrite. Results: T. cruzi cytosolic Fe-SODB is highly resistant toward peroxynitrite-mediated tyrosine nitration and inactivation as compared with mitochondrial Fe-SODA. Conclusion: Intramolecular electron transfer in Fe-SODB from Cys83 to critical Tyr35 prevents enzyme nitration and inactivation. Significance: Disparate susceptibilities of Fe-SODs to peroxynitrite can influence parasite virulence during T. cruzi infection of mammalian cells. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
author	Petruk, Ariel Alcides Martí, Marcelo Adrián Buschiazzo, Alejandro
author_facet	Petruk, Ariel Alcides Martí, Marcelo Adrián Buschiazzo, Alejandro
author_sort	Petruk, Ariel Alcides
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
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
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v289_n18_p12760_Martinez http://hdl.handle.net/20.500.12110/paper_00219258_v289_n18_p12760_Martinez
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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

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