Mostrar el registro sencillo del ítem

dc.contributor.author
Todorovic, Smilja  
dc.contributor.author
Rodrigues, João V.  
dc.contributor.author
Pinto, Ana F.  
dc.contributor.author
Thomsen, Christian  
dc.contributor.author
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  
dc.subject
Raman  
dc.subject
Redox Proteins  
dc.subject
Ion Binding  
dc.subject.classification
Otras Ciencias Químicas  
dc.subject.classification
Ciencias Químicas  
dc.subject.classification
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  
dc.description.fil
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