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dc.contributor.author
Todorovic, Smilja
dc.contributor.author
Rodrigues, João V.
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Pinto, Ana F.
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Thomsen, Christian
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Hildebrandt, Peter
dc.contributor.author
Teixeira, Miguel
dc.contributor.author
Murgida, Daniel Horacio
dc.date.available
2019-04-23T19:44:54Z
dc.date.issued
2009-12
dc.identifier.citation
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
dc.identifier.issn
1463-9076
dc.identifier.uri
http://hdl.handle.net/11336/74848
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Royal Society of Chemistry
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Superóxido Reductasa
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Raman
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Redox Proteins
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Ion Binding
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-27T17:54:12Z
dc.journal.volume
11
dc.journal.number
11
dc.journal.pagination
1809-1815
dc.journal.pais
Reino Unido
dc.description.fil
Fil: Todorovic, Smilja. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Rodrigues, João V.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Pinto, Ana F.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Thomsen, Christian. Technische Universität Berlin; Alemania
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Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania
dc.description.fil
Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal
dc.description.fil
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
dc.journal.title
Physical Chemistry Chemical Physics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1039/b815489a
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/Content/ArticleLanding/2009/CP/b815489a
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