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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/47968
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/47968
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-11-12T09:39:36Zoai: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:34982025-11-12 09:39:36.333CONICET 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
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str 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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