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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9253
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dc.contributor.authorMylonas, M.en
dc.contributor.authorMalandrinos, G.en
dc.contributor.authorPlakatouras, J.en
dc.contributor.authorHadjiliadis, N.en
dc.contributor.authorKasprzak, K. S.en
dc.contributor.authorKrezel, A.en
dc.contributor.authorBal, W.en
dc.date.accessioned2015-11-24T16:47:54Z-
dc.date.available2015-11-24T16:47:54Z-
dc.identifier.issn0893-228X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9253-
dc.rightsDefault Licence-
dc.subjectcopper(ii) complexesen
dc.subjectreduction potentialsen
dc.subjectoxygen activationen
dc.subjectpulse-radiolysisen
dc.subject3rd residueen
dc.subjectnickel(ii)en
dc.subjectbindingen
dc.subjectstabilityen
dc.subjectDNAen
dc.subjectpeptidesen
dc.titleStray Cu(II) may cause oxidative damage when coordinated to the -TESHHK- sequence derived from the C-terminal tail of histone H2Aen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1021/tx010031n-
heal.identifier.secondary<Go to ISI>://000171153800004-
heal.identifier.secondaryhttp://pubs.acs.org/doi/abs/10.1021/tx010031n-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2001-
heal.abstractCH3CO-Thr-Glu-Ser-His-His-Lys-NH2, a hexapeptide representing the 120-125 sequence of histone H2A, coordinates Cu(II) ions efficiently. Monomeric complexes are formed. In the major complex at physiological pH, CuH-1L, Cu(II) is coordinated equatorially through the imidazole nitrogen of the His-4 residue and the amide nitrogens of the Ser-3 and His-4 residues, and axially through the imidazole nitrogen of the His-5 residue. This complex reacts with H2O2 and the resulting reactive oxygen intermediate efficiently oxidizes 2 ' -deoxyguanosine. The underlying mechanism involves the formation of Cu(III) and a metal-bound hydroxyl radical species.en
heal.publisherAmerican Chemical Societyen
heal.journalNameChem Res Toxicolen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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