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dc.contributor.author
Grazina, Raquel
dc.contributor.author
Sousa, Patrícia M. Paes de
dc.contributor.author
Brondino, Carlos Dante
dc.contributor.author
Carepo, Marta S. P.
dc.contributor.author
Moura, Isabel
dc.contributor.author
Moura, José J. G.
dc.date.available
2017-04-11T17:48:08Z
dc.date.issued
2011-04
dc.identifier.citation
Grazina, Raquel; Sousa, Patrícia M. Paes de; Brondino, Carlos Dante; Carepo, Marta S. P.; Moura, Isabel; et al.; Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis; Elsevier; Bioelectrochemistry; 82; 1; 4-2011; 22-28
dc.identifier.issn
1567-5394
dc.identifier.uri
http://hdl.handle.net/11336/15146
dc.description.abstract
The redox behaviour of a ferredoxin (Fd) from Desulfovibrio alaskensis was characterized by electrochemistry. The protein was isolated and purified, and showed to be a tetramer containing one [3Fe–4S] and one [4Fe–4S] centre. This ferredoxin has high homology with FdI from Desulfovibrio vulgaris Miyazaki and Hildenborough and FdIII from Desulfovibrio africanus.
From differential pulse voltammetry the following signals were identified: [3Fe-4S]+ 1/0 (E0′ = − 158 ± 5 mV); [4Fe–4S]+ 2/+1 (E0′ = − 474 ± 5 mV) and [3Fe–4S]0/− 2 (E0′ = − 660 ± 5 mV). The effect of pH on these signals showed that the reduced [3Fe–4S]0 cluster has a pKʹred′ = 5.1 ± 0.1, the [4Fe–4S]+ 2/+1 centre is pH independent, and the [3Fe–4S]0/−2 reduction is accompanied by the binding of two protons. The ability of the [3Fe–4S]0 cluster to be converted into a new [4Fe–4S] cluster was proven. The redox potential of the original [4Fe–4S] centre showed to be dependent on the formation of the new [4Fe-4S] centre, which results in a positive shift (ca. 70 mV) of the redox potential of the original centre.
Being most [Fe–S] proteins involved in electron transport processes, the electrochemical characterization of their clusters is essential to understand their biological function. Complementary EPR studies were performed.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
7fe Ferredoxins
dc.subject
Desulfovibrio Bacteria
dc.subject
Ironsulfur Clusters
dc.subject
Electrochemistry
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
dc.subject.classification
Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-03-22T15:20:01Z
dc.journal.volume
82
dc.journal.number
1
dc.journal.pagination
22-28
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Grazina, Raquel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
dc.description.fil
Fil: Sousa, Patrícia M. Paes de. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
dc.description.fil
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; Argentina
dc.description.fil
Fil: Carepo, Marta S. P.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
dc.description.fil
Fil: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
dc.description.fil
Fil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
dc.journal.title
Bioelectrochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bioelechem.2011.04.005
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1567539411000454
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