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Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein

1999-01-01Artigo científico Acesso aberto
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dc.contributor.authorArcher, M.
dc.contributor.authorCarvalho, A. L.
dc.contributor.authorTeixeira, S.
dc.contributor.authorMoura, I.
dc.contributor.authorMoura, J. J. G.
dc.contributor.authorRusnak, F.
dc.contributor.authorRomão, Maria João
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)
dc.contributor.pblWiley-Blackwell
dc.date.accessioned2019-03-14T23:15:40Z
dc.date.available2019-03-14T23:15:40Z
dc.date.issued1999-01-01
dc.description.abstractDesulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal-substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+ derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+, and Ni2+ substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three-dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent10
dc.format.extent247230
dc.identifier.doi10.1110/ps.8.7.1536
dc.identifier.issn0961-8368
dc.identifier.otherPURE: 12115487
dc.identifier.otherPURE UUID: fa2b00ac-7dcd-4226-bc8d-28787d7135b5
dc.identifier.otherScopus: 0032805156
dc.identifier.otherPubMed: 10422844
dc.identifier.otherWOS: 000081271700019
dc.identifier.otherPubMedCentral: PMC2144384
dc.identifier.otherORCID: /0000-0002-3004-0543/work/55386327
dc.identifier.otherORCID: /0000-0002-3824-0240/work/55386442
dc.identifier.otherORCID: /0000-0002-4726-2388/work/68772322
dc.identifier.urihttp://www.scopus.com/inward/record.url?scp=0032805156&partnerID=8YFLogxK
dc.identifier.urlhttps://www.scopus.com/pages/publications/0032805156
dc.language.isoeng
dc.peerreviewedyes
dc.subjectCrystal structure
dc.subjectDesulfoferrodoxin
dc.subjectDesulforedoxin
dc.subjectIron-sulfur proteins
dc.subjectMetal substitution
dc.subjectRubredoxin-type proteins
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.titleStructural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type proteinen
dc.typejournal article
degois.publication.firstPage1536
degois.publication.issue7
degois.publication.lastPage1545
degois.publication.titleProtein Science
degois.publication.volume8
dspace.entity.typePublication
rcaap.rightsopenAccess

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