1. Ktisis Cyprus University of Technology
  2. Cyprus University of Technology (Research Output)
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Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/3171
DC FieldValueLanguage
dc.contributor.authorStylianou, Marios-
dc.contributor.authorKeramidas, Anastasios D.-
dc.contributor.authorDrouza, Chryssoula-
dc.date.accessioned2012-12-14T14:00:53Zen
dc.date.accessioned2013-05-17T07:13:06Z-
dc.date.accessioned2015-12-02T14:26:56Z-
dc.date.available2012-12-14T14:00:53Zen
dc.date.available2013-05-17T07:13:06Z-
dc.date.available2015-12-02T14:26:56Z-
dc.date.issued2010-06-08-
dc.identifier.citationBioinorganic Chemistry and Applications, 2010, vol. 2010, pp. 1-8en_US
dc.identifier.issn1687479X-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/3171-
dc.description.abstractCopper ions in the active sites of several proteins/enzymes interact with phenols and quinones, and this interaction is associated to the reactivity of the enzymes. In this study the speciation of the Cu 2+ with iminodiacetic phenolate/hydroquinonate ligands has been examined by pH-potentiometry. The results reveal that the iminodiacetic phenol ligand forms mononuclear complexes with Cu 2+ at acidic and alkaline pHs, and a binuclear O phenolate -bridged complex at pH range from 7 to 8.5. The binucleating hydroquinone ligand forms only 2:1 metal to ligand complexes in solution. The pK values of the protonation of the phenolate oxygen of the two ligands are reduced about 2 units after complexation with the metal ion and are close to the pK values for the copper-interacting tyrosine phenol oxygen in copper enzymesen_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofBioinorganic Chemistry and Applicationsen_US
dc.rights© Marios Stylianou et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectComplexesen_US
dc.subjectPhenolen_US
dc.subjectProteinsen_US
dc.subjectEnzymesen_US
dc.subjectCopper ionsen_US
dc.subjectPotentiometryen_US
dc.titlePH-potentiometric investigation towards chelating tendencies of p -hydroquinone and phenol iminodiacetate copper(II) complexesen_US
dc.typeArticleen_US
dc.collaborationUniversity of Cyprusen_US
dc.collaborationCyprus University of Technologyen_US
dc.subject.categoryBiological Sciencesen_US
dc.journalsOpen Accessen_US
dc.reviewpeer reviewed-
dc.countryCyprusen_US
dc.subject.fieldNatural Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1155/2010/125717en_US
dc.identifier.pmid20631835-
dc.dept.handle123456789/70en
dc.relation.volume2010en_US
cut.common.academicyear2010-2011en_US
dc.identifier.spage1en_US
dc.identifier.epage8en_US
item.fulltextWith Fulltext-
item.cerifentitytypePublications-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.languageiso639-1en-
crisitem.journal.journalissn1687-479X-
crisitem.journal.publisherHindawi-
crisitem.author.deptDepartment of Agricultural Sciences, Biotechnology and Food Science-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0002-2630-4323-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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