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The role of the hybrid cluster protein in oxidative stress defense

2006-10-27Artigo científico Acesso aberto
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dc.contributor.authorAlmeida, Cláudia C.
dc.contributor.authorRomão, Célia V.
dc.contributor.authorLindley, Peter F.
dc.contributor.authorTeixeira, Miguel
dc.contributor.authorSaraiva, Lígia M.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblASBMB - American Society for Biochemistry and Molecular Biology
dc.date.accessioned2025-12-02T21:00:24Z
dc.date.available2025-12-02T21:00:24Z
dc.date.issued2006-10-27
dc.description.abstractHybrid cluster proteins (HCP) contain two types of Fe/S clusters, namely a [4Fe-4S]2+/1+ or [2Fe-2S]2+/1+ cluster and a novel type of hybrid cluster, [4Fe-2S-2O], in the as-isolated state. Although first isolated from anaerobic sulfate-reducing bacteria, the analysis of the genomic sequences reveals that genes encoding putative hybrid cluster proteins are present in a wide range of organisms, aerobic, anaerobic, or facultative, from the Bacteria, Archaea, and Eukarya domains. Despite a detailed spectroscopic and structural characterization, the precise physiological function of these proteins remained unknown. The present work shows that the transcription of the Escherichia coli hcp gene is induced by hydrogen peroxide, and this induction is regulated by the redox-sensitive transcriptional activator, OxyR. The E. coli hcp mutant strain exhibits higher sensitivity to hydrogen peroxide, a behavior that reverts to the wild type phenotype once a plasmid carrying the hcp gene is reintroduced. Furthermore, the purified HCPs from E. coli and Desulfovibrio desulfuricans ATCC 27774 show an alternative enzymatic activity, which under physiological conditions exhibited Km values for hydrogen peroxide (∼0.3 mM) within the range of other peroxidases. Altogether, the results reveal that HCP is involved in oxidative stress protection.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent6
dc.format.extent827871
dc.identifier.doi10.1074/jbc.M605888200
dc.identifier.issn0021-9258
dc.identifier.otherPURE: 14921447
dc.identifier.otherPURE UUID: e3af38cd-5bba-46b2-8b38-9b546abd12d9
dc.identifier.otherScopus: 33845930533
dc.identifier.otherPubMed: 16928682
dc.identifier.otherWOS: 000241414500042
dc.identifier.urihttp://hdl.handle.net/10362/191402
dc.identifier.urlhttps://www.scopus.com/pages/publications/33845930533
dc.language.isoeng
dc.peerreviewedyes
dc.subjectDesulfovibrio desulfuricans
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectGene Deletion
dc.subjectGenes, Bacterial
dc.subjectGenetic Complementation Test
dc.subjectHydrogen Peroxide
dc.subjectIron-Sulfur Proteins
dc.subjectModels, Chemical
dc.subjectOxidants
dc.subjectOxidation-Reduction
dc.subjectOxidative Stress
dc.subjectPlasmids
dc.subjectRecombinant Proteins
dc.subjectRegulon
dc.subjectTrans-Activators
dc.subjectTranscription, Genetic
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectCell Biology
dc.titleThe role of the hybrid cluster protein in oxidative stress defenseen
dc.typejournal article
degois.publication.firstPage32445
degois.publication.issue43
degois.publication.lastPage32450
degois.publication.titleJournal of Biological Chemistry
degois.publication.volume281
dspace.entity.typePublication
rcaap.rightsopenAccess

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