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Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster

dc.contributor.authorRodrigues, Pedro M.
dc.contributor.authorMacedo, Anjos L.
dc.contributor.authorMoura, Isabel
dc.contributor.authorMoura, José J. G.
dc.contributor.authorGoodfellow, Brian J.
dc.date.accessioned2013-02-06T11:45:46Z
dc.date.available2013-02-06T11:45:46Z
dc.date.issued2006
dc.descriptionJ Biol Inorg Chem (2006) 11: 307–315 DOI 10.1007/s00775-005-0077-2por
dc.description.abstractDesulfovibrio gigas ferredoxin II (DgFdII) is a small protein with a polypeptide chain composed of 58 amino acids, containing one Fe3S4 cluster per monomer. Upon studying the redox cycle of this protein, we detected a stable intermediate (FdIIint) with four 1H resonances at 24.1, 20.5, 20.8 and 13.7 ppm. The differences between FdIIox and FdIIint were attributed to conformational changes resulting from the breaking/formation of an internal disulfide bridge. The same 1H NMR methodology used to fully assign the three cysteinyl ligands of the [3Fe-4S] core in the oxidized state (DgFdIIox) was used here for the assignment of the same three ligands in the intermediate state (DgFdIIint). The spin-coupling model used for the oxidized form of DgFdII where magnetic exchange coupling constants of around 300 cm-1 and hyperfine coupling constants equal to 1 MHz for all the three iron centres were found, does not explain the isotropic shift temperature dependence for the three cysteinyl cluster ligands in DgFdIIint. This study, together with the spin delocalization mechanism proposed here for DgFdIIint, allows the detection of structural modifications at the [3Fe-4S] cluster in DgFdIIox and DgFdIIint.por
dc.identifier.issn0949-8257
dc.identifier.urihttp://hdl.handle.net/10362/8710
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherSpringerpor
dc.relation.publisherversionhttp://link.springer.com/article/10.1007%2Fs00775-005-0077-2por
dc.titleDesulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] clusterpor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage315por
oaire.citation.startPage307por
oaire.citation.titleJBIC Journal of Biological Inorganic Chemistrypor
oaire.citation.volume11por
rcaap.rightsopenAccesspor
rcaap.typearticlepor

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