Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects

Autores
Iglesias, Dario Ezequiel; Bombicino, Silvina Sonia; Valdez, Laura Batriz; Boveris, Alberto Antonio
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of NO between cytochromes b and c of the mitochondrial respiratory chain were studied using submitochondrial particles (SMP) from bovine heart and GSNO and SPER-NO as NO sources. Succinate-cytochrome c reductase (complex II-III) activity (222±4 nmol/min. mg protein) was inhibited by 51% in the presence of 500 μM GSNO and by 48% in the presence of 30 μM SPER-NO, in both cases at ~1.25 μM NO. Neither GSNO nor SPER-NO were able to inhibit succinate-Q reductase activity (complex II; 220±9 nmol/min. mg protein), showing that NO affects complex III. Complex II-III activity was decreased (36%) when SMP were incubated with l-arginine and mtNOS cofactors, indicating that this effect is also produced by endogenous NO. GSNO (500 μM) reduced cytochrome b562 by 71%, in an [O2] independent manner. Hyperbolic increases in O2 •- (up to 1.3±0.1 nmol/min. mg protein) and H2O2 (up to 0.64±0.05 nmol/min. mg protein) productions were observed with a maximal effect at 500 μM GSNO. The O2 •-/H2O2 ratio was 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. Moreover, H2O2 production was increased by 72-74% when heart coupled mitochondria were exposed to 500 μM GSNO or 30 μM SPER-NO. SMP incubated in the presence of succinate showed an EPR signal (g=1.99) compatible with a stable semiquinone. This EPR signal was increased not only by antimycin but also by GSNO and SPER-NO. These signals were not modified under N2 atmosphere, indicating that they are not a consequence to the effect of NOx species on complex III area. These results show that NO interacts with ubiquinone-cytochrome b area producing antimycin-like effects. This behaviour comprises the inhibition of electron transfer, the interruption of the oxidation of cytochromes b, and the enhancement of [UQH•]ss which, in turn, leads to an increase in O2 •- and H2O2 mitochondrial production rates.
Fil: Iglesias, Dario Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
Fil: Bombicino, Silvina Sonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; 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 de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
Fil: Boveris, Alberto Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
Materia
Cytochrome Bc1 Complex
Electron Paramagnetic Resonance (Epr)
Hydrogen Peroxide
Nitric Oxide
S-Nitrosoglutathione (Gsno)
Spermine-Nonoate (Sper-No)
Superoxide Anion
Ubiquinone-Cytochrome B Area
Ubisemiquinone
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/38835
Acceder
id CONICETDig_3dbb5b75f867a0216e149d9e59a19aed
oai_identifier_str oai:ri.conicet.gov.ar:11336/38835
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Nitric oxide interacts with mitochondrial complex III producing antimycin-like effectsIglesias, Dario EzequielBombicino, Silvina SoniaValdez, Laura BatrizBoveris, Alberto AntonioCytochrome Bc1 ComplexElectron Paramagnetic Resonance (Epr)Hydrogen PeroxideNitric OxideS-Nitrosoglutathione (Gsno)Spermine-Nonoate (Sper-No)Superoxide AnionUbiquinone-Cytochrome B AreaUbisemiquinonehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The effect of NO between cytochromes b and c of the mitochondrial respiratory chain were studied using submitochondrial particles (SMP) from bovine heart and GSNO and SPER-NO as NO sources. Succinate-cytochrome c reductase (complex II-III) activity (222±4 nmol/min. mg protein) was inhibited by 51% in the presence of 500 μM GSNO and by 48% in the presence of 30 μM SPER-NO, in both cases at ~1.25 μM NO. Neither GSNO nor SPER-NO were able to inhibit succinate-Q reductase activity (complex II; 220±9 nmol/min. mg protein), showing that NO affects complex III. Complex II-III activity was decreased (36%) when SMP were incubated with l-arginine and mtNOS cofactors, indicating that this effect is also produced by endogenous NO. GSNO (500 μM) reduced cytochrome b562 by 71%, in an [O2] independent manner. Hyperbolic increases in O2 •- (up to 1.3±0.1 nmol/min. mg protein) and H2O2 (up to 0.64±0.05 nmol/min. mg protein) productions were observed with a maximal effect at 500 μM GSNO. The O2 •-/H2O2 ratio was 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. Moreover, H2O2 production was increased by 72-74% when heart coupled mitochondria were exposed to 500 μM GSNO or 30 μM SPER-NO. SMP incubated in the presence of succinate showed an EPR signal (g=1.99) compatible with a stable semiquinone. This EPR signal was increased not only by antimycin but also by GSNO and SPER-NO. These signals were not modified under N2 atmosphere, indicating that they are not a consequence to the effect of NOx species on complex III area. These results show that NO interacts with ubiquinone-cytochrome b area producing antimycin-like effects. This behaviour comprises the inhibition of electron transfer, the interruption of the oxidation of cytochromes b, and the enhancement of [UQH•]ss which, in turn, leads to an increase in O2 •- and H2O2 mitochondrial production rates.Fil: Iglesias, Dario Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; ArgentinaFil: Bombicino, Silvina Sonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; 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 de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; ArgentinaFil: Boveris, Alberto Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; ArgentinaElsevier Science Inc2015-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/38835Iglesias, Dario Ezequiel; Bombicino, Silvina Sonia; Valdez, Laura Batriz; Boveris, Alberto Antonio; Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects; Elsevier Science Inc; Free Radical Biology and Medicine; 89; 12-2015; 602-6130891-5849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2015.08.024info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0891584915005997info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:08:28Zoai:ri.conicet.gov.ar:11336/38835instacron: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 10:08:28.406CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
title Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
spellingShingle Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
Iglesias, Dario Ezequiel
Cytochrome Bc1 Complex
Electron Paramagnetic Resonance (Epr)
Hydrogen Peroxide
Nitric Oxide
S-Nitrosoglutathione (Gsno)
Spermine-Nonoate (Sper-No)
Superoxide Anion
Ubiquinone-Cytochrome B Area
Ubisemiquinone
title_short Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
title_full Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
title_fullStr Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
title_full_unstemmed Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
title_sort Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
dc.creator.none.fl_str_mv Iglesias, Dario Ezequiel
Bombicino, Silvina Sonia
Valdez, Laura Batriz
Boveris, Alberto Antonio
author Iglesias, Dario Ezequiel
author_facet Iglesias, Dario Ezequiel
Bombicino, Silvina Sonia
Valdez, Laura Batriz
Boveris, Alberto Antonio
author_role author
author2 Bombicino, Silvina Sonia
Valdez, Laura Batriz
Boveris, Alberto Antonio
author2_role author
author
author
dc.subject.none.fl_str_mv Cytochrome Bc1 Complex
Electron Paramagnetic Resonance (Epr)
Hydrogen Peroxide
Nitric Oxide
S-Nitrosoglutathione (Gsno)
Spermine-Nonoate (Sper-No)
Superoxide Anion
Ubiquinone-Cytochrome B Area
Ubisemiquinone
topic Cytochrome Bc1 Complex
Electron Paramagnetic Resonance (Epr)
Hydrogen Peroxide
Nitric Oxide
S-Nitrosoglutathione (Gsno)
Spermine-Nonoate (Sper-No)
Superoxide Anion
Ubiquinone-Cytochrome B Area
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 The effect of NO between cytochromes b and c of the mitochondrial respiratory chain were studied using submitochondrial particles (SMP) from bovine heart and GSNO and SPER-NO as NO sources. Succinate-cytochrome c reductase (complex II-III) activity (222±4 nmol/min. mg protein) was inhibited by 51% in the presence of 500 μM GSNO and by 48% in the presence of 30 μM SPER-NO, in both cases at ~1.25 μM NO. Neither GSNO nor SPER-NO were able to inhibit succinate-Q reductase activity (complex II; 220±9 nmol/min. mg protein), showing that NO affects complex III. Complex II-III activity was decreased (36%) when SMP were incubated with l-arginine and mtNOS cofactors, indicating that this effect is also produced by endogenous NO. GSNO (500 μM) reduced cytochrome b562 by 71%, in an [O2] independent manner. Hyperbolic increases in O2 •- (up to 1.3±0.1 nmol/min. mg protein) and H2O2 (up to 0.64±0.05 nmol/min. mg protein) productions were observed with a maximal effect at 500 μM GSNO. The O2 •-/H2O2 ratio was 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. Moreover, H2O2 production was increased by 72-74% when heart coupled mitochondria were exposed to 500 μM GSNO or 30 μM SPER-NO. SMP incubated in the presence of succinate showed an EPR signal (g=1.99) compatible with a stable semiquinone. This EPR signal was increased not only by antimycin but also by GSNO and SPER-NO. These signals were not modified under N2 atmosphere, indicating that they are not a consequence to the effect of NOx species on complex III area. These results show that NO interacts with ubiquinone-cytochrome b area producing antimycin-like effects. This behaviour comprises the inhibition of electron transfer, the interruption of the oxidation of cytochromes b, and the enhancement of [UQH•]ss which, in turn, leads to an increase in O2 •- and H2O2 mitochondrial production rates.
Fil: Iglesias, Dario Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
Fil: Bombicino, Silvina Sonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; 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 de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
Fil: Boveris, Alberto Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina
description The effect of NO between cytochromes b and c of the mitochondrial respiratory chain were studied using submitochondrial particles (SMP) from bovine heart and GSNO and SPER-NO as NO sources. Succinate-cytochrome c reductase (complex II-III) activity (222±4 nmol/min. mg protein) was inhibited by 51% in the presence of 500 μM GSNO and by 48% in the presence of 30 μM SPER-NO, in both cases at ~1.25 μM NO. Neither GSNO nor SPER-NO were able to inhibit succinate-Q reductase activity (complex II; 220±9 nmol/min. mg protein), showing that NO affects complex III. Complex II-III activity was decreased (36%) when SMP were incubated with l-arginine and mtNOS cofactors, indicating that this effect is also produced by endogenous NO. GSNO (500 μM) reduced cytochrome b562 by 71%, in an [O2] independent manner. Hyperbolic increases in O2 •- (up to 1.3±0.1 nmol/min. mg protein) and H2O2 (up to 0.64±0.05 nmol/min. mg protein) productions were observed with a maximal effect at 500 μM GSNO. The O2 •-/H2O2 ratio was 1.98 in accordance with the stoichiometry of the O2 •- disproportionation. Moreover, H2O2 production was increased by 72-74% when heart coupled mitochondria were exposed to 500 μM GSNO or 30 μM SPER-NO. SMP incubated in the presence of succinate showed an EPR signal (g=1.99) compatible with a stable semiquinone. This EPR signal was increased not only by antimycin but also by GSNO and SPER-NO. These signals were not modified under N2 atmosphere, indicating that they are not a consequence to the effect of NOx species on complex III area. These results show that NO interacts with ubiquinone-cytochrome b area producing antimycin-like effects. This behaviour comprises the inhibition of electron transfer, the interruption of the oxidation of cytochromes b, and the enhancement of [UQH•]ss which, in turn, leads to an increase in O2 •- and H2O2 mitochondrial production rates.
publishDate 2015
dc.date.none.fl_str_mv 2015-12
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/11336/38835
Iglesias, Dario Ezequiel; Bombicino, Silvina Sonia; Valdez, Laura Batriz; Boveris, Alberto Antonio; Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects; Elsevier Science Inc; Free Radical Biology and Medicine; 89; 12-2015; 602-613
0891-5849
CONICET Digital
CONICET
url http://hdl.handle.net/11336/38835
identifier_str_mv Iglesias, Dario Ezequiel; Bombicino, Silvina Sonia; Valdez, Laura Batriz; Boveris, Alberto Antonio; Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects; Elsevier Science Inc; Free Radical Biology and Medicine; 89; 12-2015; 602-613
0891-5849
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2015.08.024
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0891584915005997
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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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score 13.070432

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