Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6552
DC FieldValueLanguage
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorDaskalakis, Vangelis-
dc.date.accessioned2013-01-16T13:45:50Zen
dc.date.accessioned2013-05-17T07:13:15Z-
dc.date.accessioned2015-12-02T14:27:34Z-
dc.date.available2013-01-16T13:45:50Zen
dc.date.available2013-05-17T07:13:15Z-
dc.date.available2015-12-02T14:27:34Z-
dc.date.issued2012-04-
dc.identifier.citationBiochimica et Biophysica acta - Bioenergetics, 2012, vol.1817, no.4, pp. 552-557en_US
dc.identifier.issn0005-2728-
dc.description.abstractThe dioxygen reduction mechanism in cytochrome oxidases relies on proton control of the electron transfer events that drive the process. Proton delivery and proton channels in the protein that are relevant to substrate reduction and proton pumping are considered, and the current status of this area is summarized. We propose a mechanism in which the coupling of the oxygen reduction chemistry to proton translocation (P → F transition) is related to the properties of two groups of highly conserved residues, namely, His411/G386-T389 and the heme a 3-propionateA-D399-H403 chain. This article is part of a Special Issue entitled: Respiratory Oxidasesen_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.publisherElsevieren
dc.relation.ispartofBiochimica et Biophysica Acta - Bioenergeticsen_US
dc.rights© 2011 Elsevieren_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectCopperen_US
dc.subjectHemeen_US
dc.subjectHydrogen peroxideen_US
dc.subjectOxidoreductasesen_US
dc.subjectOxygenen_US
dc.subjectBacterial Proteinsen_US
dc.subjectBiological transporten_US
dc.subjectProtonsen_US
dc.subjectSpectrum analysisen_US
dc.titleThe origin of the FeIV = O intermediates in cytochrome aa3 oxidaseen_US
dc.typeArticleen_US
dc.collaborationCyprus University of Technologyen_US
dc.collaborationUniversity of Cyprusen_US
dc.journalsOpen Accessen_US
dc.reviewpeer reviewed-
dc.countryCyprusen_US
dc.subject.fieldAgricultural Sciencesen_US
dc.identifier.doi10.1016/j.bbabio.2011.07.009en_US
dc.dept.handle123456789/70en
dc.relation.issue4en_US
dc.relation.volume1817en_US
cut.common.academicyear2011-2012en_US
dc.identifier.spage552en_US
dc.identifier.epage557en_US
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairetypearticle-
item.cerifentitytypePublications-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.orcid0000-0001-8870-0850-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.journal.journalissn0005-2728-
crisitem.journal.publisherElsevier-
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