Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'
- Autores
- Todorovic, Smilja; Rodrigues, João V.; Pinto, Ana F.; Thomsen, Christian; Hildebrandt, Peter; Teixeira, Miguel; Murgida, Daniel Horacio
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a ′natural variant′. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH.
Fil: Todorovic, Smilja. Universidade Nova de Lisboa; Portugal
Fil: Rodrigues, João V.. Universidade Nova de Lisboa; Portugal
Fil: Pinto, Ana F.. Universidade Nova de Lisboa; Portugal
Fil: Thomsen, Christian. Technische Universität Berlin; Alemania
Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania
Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal
Fil: Murgida, Daniel Horacio. 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 - Materia
-
Superóxido Reductasa
Raman
Redox Proteins
Ion Binding - 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:11336/74848
Ver los metadatos del registro completo
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Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'Todorovic, SmiljaRodrigues, João V.Pinto, Ana F.Thomsen, ChristianHildebrandt, PeterTeixeira, MiguelMurgida, Daniel HoracioSuperóxido ReductasaRamanRedox ProteinsIon Bindinghttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a ′natural variant′. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH.Fil: Todorovic, Smilja. Universidade Nova de Lisboa; PortugalFil: Rodrigues, João V.. Universidade Nova de Lisboa; PortugalFil: Pinto, Ana F.. Universidade Nova de Lisboa; PortugalFil: Thomsen, Christian. Technische Universität Berlin; AlemaniaFil: Hildebrandt, Peter. Technische Universität Berlin; AlemaniaFil: Teixeira, Miguel. Universidade Nova de Lisboa; PortugalFil: Murgida, Daniel Horacio. 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; ArgentinaRoyal Society of Chemistry2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/74848Todorovic, Smilja; Rodrigues, João V.; Pinto, Ana F.; Thomsen, Christian; Hildebrandt, Peter; et al.; Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 11; 12-2009; 1809-18151463-9076CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/b815489ainfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/Content/ArticleLanding/2009/CP/b815489ainfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:10:15Zoai:ri.conicet.gov.ar:11336/74848instacron: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 10:10:16.194CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
title |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
spellingShingle |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' Todorovic, Smilja Superóxido Reductasa Raman Redox Proteins Ion Binding |
title_short |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
title_full |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
title_fullStr |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
title_full_unstemmed |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
title_sort |
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
dc.creator.none.fl_str_mv |
Todorovic, Smilja Rodrigues, João V. Pinto, Ana F. Thomsen, Christian Hildebrandt, Peter Teixeira, Miguel Murgida, Daniel Horacio |
author |
Todorovic, Smilja |
author_facet |
Todorovic, Smilja Rodrigues, João V. Pinto, Ana F. Thomsen, Christian Hildebrandt, Peter Teixeira, Miguel Murgida, Daniel Horacio |
author_role |
author |
author2 |
Rodrigues, João V. Pinto, Ana F. Thomsen, Christian Hildebrandt, Peter Teixeira, Miguel Murgida, Daniel Horacio |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Superóxido Reductasa Raman Redox Proteins Ion Binding |
topic |
Superóxido Reductasa Raman Redox Proteins Ion Binding |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a ′natural variant′. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH. Fil: Todorovic, Smilja. Universidade Nova de Lisboa; Portugal Fil: Rodrigues, João V.. Universidade Nova de Lisboa; Portugal Fil: Pinto, Ana F.. Universidade Nova de Lisboa; Portugal Fil: Thomsen, Christian. Technische Universität Berlin; Alemania Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal Fil: Murgida, Daniel Horacio. 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 |
description |
The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a ′natural variant′. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-12 |
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/11336/74848 Todorovic, Smilja; Rodrigues, João V.; Pinto, Ana F.; Thomsen, Christian; Hildebrandt, Peter; et al.; Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 11; 12-2009; 1809-1815 1463-9076 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/74848 |
identifier_str_mv |
Todorovic, Smilja; Rodrigues, João V.; Pinto, Ana F.; Thomsen, Christian; Hildebrandt, Peter; et al.; Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 11; 12-2009; 1809-1815 1463-9076 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1039/b815489a info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/Content/ArticleLanding/2009/CP/b815489a |
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 |
dc.publisher.none.fl_str_mv |
Royal Society of Chemistry |
publisher.none.fl_str_mv |
Royal Society of Chemistry |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1844613989799034880 |
score |
13.070432 |