Superoxide and hydrogen peroxide productions by NO-inhibited complex III
- Autores
- Iglesias, Darío E.; Bombicino, Silvina Sonia; Boveris, Alberto Antonio; Valdez, Laura Batriz
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Complex III plays a central role in the mitochondrial respiratory chain transferring electrons from ubiquinol to cytochrome c and pumping protons to the intermembrane space, contributing to the protonmotive force. Furthermore, complex III can act as a source of O2 •- in the presence of ubiquinol and antimycin, an expermiental condition in which the oxidation of the cytochrome b hemes is blocked. The O2 •- dismutation catalyzed by superoxide dismutase produces H2O2, a known second messenger in redox signalling. Results from our laboratory have shown that NO, released from GSNO or from SPER -NO or generated by mtNOS, inhibits electron transfer at ubiquinone-cytochrome b area producing antimycin-like effects. Thus, both antimycin- and NO-inhibited complex III showed a high content of cytochromes b in the reduced state (79 and 71%, respectively) and an enhancement in the ubisemiquinone EPR signal at g=1.99 (42 and 35%, respectively). As consequence, O2 •- and H2O2 productions were increased, being the O2 •-/H2O2 ratio equal to 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. The interruption of the oxidation of cytochromes b by NO leads to an enhancement of the steady-state concentration of UQH• , allowing cytochrome bc1 complex to act as a source of reactive oxygen species in physiological conditions.
Fil: Iglesias, Darío E.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina
Fil: Bombicino, Silvina Sonia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina
Fil: Boveris, Alberto Antonio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Valdez, Laura Batriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina - Materia
-
S-NITROSOGLUTATHIONE
SPERMINE-NONOATE
ELECTRON PARAMAGNETIC RESONANCE
UBISEMIQUINONE - 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:11336/47968
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Superoxide and hydrogen peroxide productions by NO-inhibited complex IIIIglesias, Darío E.Bombicino, Silvina SoniaBoveris, Alberto AntonioValdez, Laura BatrizS-NITROSOGLUTATHIONESPERMINE-NONOATEELECTRON PARAMAGNETIC RESONANCEUBISEMIQUINONEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Complex III plays a central role in the mitochondrial respiratory chain transferring electrons from ubiquinol to cytochrome c and pumping protons to the intermembrane space, contributing to the protonmotive force. Furthermore, complex III can act as a source of O2 •- in the presence of ubiquinol and antimycin, an expermiental condition in which the oxidation of the cytochrome b hemes is blocked. The O2 •- dismutation catalyzed by superoxide dismutase produces H2O2, a known second messenger in redox signalling. Results from our laboratory have shown that NO, released from GSNO or from SPER -NO or generated by mtNOS, inhibits electron transfer at ubiquinone-cytochrome b area producing antimycin-like effects. Thus, both antimycin- and NO-inhibited complex III showed a high content of cytochromes b in the reduced state (79 and 71%, respectively) and an enhancement in the ubisemiquinone EPR signal at g=1.99 (42 and 35%, respectively). As consequence, O2 •- and H2O2 productions were increased, being the O2 •-/H2O2 ratio equal to 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. The interruption of the oxidation of cytochromes b by NO leads to an enhancement of the steady-state concentration of UQH• , allowing cytochrome bc1 complex to act as a source of reactive oxygen species in physiological conditions.Fil: Iglesias, Darío E.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; ArgentinaFil: Bombicino, Silvina Sonia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; ArgentinaFil: Boveris, Alberto Antonio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Valdez, Laura Batriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; ArgentinaSociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas2016-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/47968Iglesias, Darío E.; Bombicino, Silvina Sonia; Boveris, Alberto Antonio; Valdez, Laura Batriz; Superoxide and hydrogen peroxide productions by NO-inhibited complex III; Sociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas; Biocell; 40; 1; 4-2016; 27-301667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mendoza-conicet.gob.ar/portal/biocell/vol/pdf/40_1/Biocell_MS5007_Iglesias.pdfinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:45:48Zoai:ri.conicet.gov.ar:11336/47968instacron: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 09:45:48.969CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
title |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
spellingShingle |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III Iglesias, Darío E. S-NITROSOGLUTATHIONE SPERMINE-NONOATE ELECTRON PARAMAGNETIC RESONANCE UBISEMIQUINONE |
title_short |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
title_full |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
title_fullStr |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
title_full_unstemmed |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
title_sort |
Superoxide and hydrogen peroxide productions by NO-inhibited complex III |
dc.creator.none.fl_str_mv |
Iglesias, Darío E. Bombicino, Silvina Sonia Boveris, Alberto Antonio Valdez, Laura Batriz |
author |
Iglesias, Darío E. |
author_facet |
Iglesias, Darío E. Bombicino, Silvina Sonia Boveris, Alberto Antonio Valdez, Laura Batriz |
author_role |
author |
author2 |
Bombicino, Silvina Sonia Boveris, Alberto Antonio Valdez, Laura Batriz |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
S-NITROSOGLUTATHIONE SPERMINE-NONOATE ELECTRON PARAMAGNETIC RESONANCE UBISEMIQUINONE |
topic |
S-NITROSOGLUTATHIONE SPERMINE-NONOATE ELECTRON PARAMAGNETIC RESONANCE UBISEMIQUINONE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Complex III plays a central role in the mitochondrial respiratory chain transferring electrons from ubiquinol to cytochrome c and pumping protons to the intermembrane space, contributing to the protonmotive force. Furthermore, complex III can act as a source of O2 •- in the presence of ubiquinol and antimycin, an expermiental condition in which the oxidation of the cytochrome b hemes is blocked. The O2 •- dismutation catalyzed by superoxide dismutase produces H2O2, a known second messenger in redox signalling. Results from our laboratory have shown that NO, released from GSNO or from SPER -NO or generated by mtNOS, inhibits electron transfer at ubiquinone-cytochrome b area producing antimycin-like effects. Thus, both antimycin- and NO-inhibited complex III showed a high content of cytochromes b in the reduced state (79 and 71%, respectively) and an enhancement in the ubisemiquinone EPR signal at g=1.99 (42 and 35%, respectively). As consequence, O2 •- and H2O2 productions were increased, being the O2 •-/H2O2 ratio equal to 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. The interruption of the oxidation of cytochromes b by NO leads to an enhancement of the steady-state concentration of UQH• , allowing cytochrome bc1 complex to act as a source of reactive oxygen species in physiological conditions. Fil: Iglesias, Darío E.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina Fil: Bombicino, Silvina Sonia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina Fil: Boveris, Alberto Antonio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Valdez, Laura Batriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica; Argentina |
description |
Complex III plays a central role in the mitochondrial respiratory chain transferring electrons from ubiquinol to cytochrome c and pumping protons to the intermembrane space, contributing to the protonmotive force. Furthermore, complex III can act as a source of O2 •- in the presence of ubiquinol and antimycin, an expermiental condition in which the oxidation of the cytochrome b hemes is blocked. The O2 •- dismutation catalyzed by superoxide dismutase produces H2O2, a known second messenger in redox signalling. Results from our laboratory have shown that NO, released from GSNO or from SPER -NO or generated by mtNOS, inhibits electron transfer at ubiquinone-cytochrome b area producing antimycin-like effects. Thus, both antimycin- and NO-inhibited complex III showed a high content of cytochromes b in the reduced state (79 and 71%, respectively) and an enhancement in the ubisemiquinone EPR signal at g=1.99 (42 and 35%, respectively). As consequence, O2 •- and H2O2 productions were increased, being the O2 •-/H2O2 ratio equal to 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. The interruption of the oxidation of cytochromes b by NO leads to an enhancement of the steady-state concentration of UQH• , allowing cytochrome bc1 complex to act as a source of reactive oxygen species in physiological conditions. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-04 |
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/11336/47968 Iglesias, Darío E.; Bombicino, Silvina Sonia; Boveris, Alberto Antonio; Valdez, Laura Batriz; Superoxide and hydrogen peroxide productions by NO-inhibited complex III; Sociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas; Biocell; 40; 1; 4-2016; 27-30 1667-5746 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/47968 |
identifier_str_mv |
Iglesias, Darío E.; Bombicino, Silvina Sonia; Boveris, Alberto Antonio; Valdez, Laura Batriz; Superoxide and hydrogen peroxide productions by NO-inhibited complex III; Sociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas; Biocell; 40; 1; 4-2016; 27-30 1667-5746 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.mendoza-conicet.gob.ar/portal/biocell/vol/pdf/40_1/Biocell_MS5007_Iglesias.pdf |
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/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Sociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas |
publisher.none.fl_str_mv |
Sociedad Latinoamericana de Microscopía Electrónica; Centro Regional de Investigaciones Científicas y Tecnológicas |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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1844613432198823936 |
score |
13.070432 |