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dc.contributor.authorTamarit Sumalla, Jordi
dc.contributor.authorGerez, Catherine
dc.contributor.authorMeier, Christian
dc.contributor.authorMulliez, Etienne
dc.contributor.authorTrautwein, Alfred
dc.contributor.authorFontecave, Marc
dc.date.accessioned2016-03-30T08:25:41Z
dc.date.available2016-03-30T08:25:41Z
dc.date.issued2000
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/10459.1/56769
dc.description.abstractClass III anaerobic ribonucleotide reductase small component, named protein b, contains a (4Fe-4S) center. Its function is to mediate electron transfer from reduced flavodoxin to S-adenosylmethionine, required for the introduction of a glycyl radical in the large component, named protein a, which then becomes active for the reduction of ribonucleotides. By site-directed mutagenesis we demonstrate that the three cysteines of the conserved CXXXCXXC sequence are involved in iron chelation. Such a sequence is also present in the activase of the pyruvate formate-lyase and in the biotin synthase, both carrying an iron-sulfur center involved in reductive activation of S-adenosylmethionine. Even though they are able to bind iron in the (4Fe-4S) form, as shown by Mo¨ssbauer spectroscopy, the corresponding Cys to Ala mutants are catalytically inactive. Mutation of the two other cysteines of the protein did not result in inactivation. We thus conclude that the (4Fe-4S) cluster has, in the wild type protein, only three cysteine ligands and a fourth still unidentified ligand.ca_ES
dc.language.isoengca_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1074/jbc.275.21.15669ca_ES
dc.relation.ispartofJournal of Biological Chemistry, 2000, Vol. 275, núm. 21, p. 15669-15675ca_ES
dc.rights(c) The American Society for Biochemistry and Molecular Biology, 2000ca_ES
dc.titleThe Activating Component of the Anaerobic Ribonucleotide Reductase from Escherichia colica_ES
dc.typearticleca_ES
dc.identifier.idgrec005704
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1074/jbc.275.21.15669


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