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dc.contributor.authorSanchuki, Heloisa BS
dc.contributor.authorValdameri, Glaucio
dc.contributor.authorMoure, Vivian R
dc.contributor.authorRodriguez, Jorge A
dc.contributor.authorPedrosa, Fabio O
dc.contributor.authorSouza, Emanuel M
dc.contributor.authorKorolik, Victoria
dc.contributor.authorRibeiro, Ronny Rocha
dc.contributor.authorHuergo, Luciano F
dc.date.accessioned2019-02-28T06:54:55Z
dc.date.available2019-02-28T06:54:55Z
dc.date.issued2016
dc.identifier.issn1350-0872
dc.identifier.doi10.1099/mic.0.000210
dc.identifier.urihttp://hdl.handle.net/10072/142443
dc.description.abstractIron is an essential micronutrient for living organisms as it is involved in a broad variety of important biological processes. However, free iron inside the cell could be potentially toxic, generating hydroxyl radicals through the Fenton reaction. Dps (DNA-binding protein from starved cells) belongs to a subfamily of ferritins and can store iron atoms inside the dodecamer. The presence of a ferroxidase centre, composed of highly conserved residues, is a signature of this protein family. In this study, we analysed the role of two conserved histidine residues (H25 and H37) located at the ferroxidase centre of the Campylobacter jejuni Dps protein by replacing them with glycine residues. The C. jejuni H25G/H37G substituted variant showed reduced iron binding and ferroxidase activities in comparison with wt Dps, while DNA-binding activity remained unaffected. We also found that both CjDps wt and CjDps H25G/H37G were able to bind manganese atoms. These results indicate that the H25 and H37 residues at the ferroxidase centre of C. jejuni Dps are not strictly required for metal binding and oxidation.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherSociety for General Microbiology
dc.relation.ispartofpagefrom156
dc.relation.ispartofpageto163
dc.relation.ispartofjournalMicrobiology
dc.relation.ispartofvolume162
dc.subject.fieldofresearchMedical Microbiology not elsewhere classified
dc.subject.fieldofresearchcode110899
dc.subject.keywordsHistidine residues
dc.subject.keywordsCampylobacter jejuni
dc.subject.keywordsDps protein
dc.subject.keywordsMetal binding
dc.subject.keywordsOxidation
dc.titleConserved histidine residues at the ferroxidase centre of the Campylobacter jejuni Dps protein are not strictly required for metal binding and oxidation
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorKorolik, Victoria
gro.griffith.authorHuergo, Luciano


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