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dc.contributor.authorPinakoulaki, Eftychiaen
dc.contributor.authorDaskalakis, Vangelisen
dc.contributor.authorVarotsis, Constantinosen
dc.creatorPinakoulaki, Eftychiaen
dc.creatorDaskalakis, Vangelisen
dc.creatorVarotsis, Constantinosen
dc.date.accessioned2019-11-21T06:22:18Z
dc.date.available2019-11-21T06:22:18Z
dc.date.issued2012
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/56025
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 Oxidases. © 2011 Elsevier B.V. All rights reserved.en
dc.sourceBiochimica et Biophysica Acta - Bioenergeticsen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84857920643&doi=10.1016%2fj.bbabio.2011.07.009&partnerID=40&md5=620d263e39a5d48cef81ce23ddefe420
dc.subjectarticleen
dc.subjectpriority journalen
dc.subjectunclassified drugen
dc.subjectenzyme activityen
dc.subjectIronen
dc.subjectmolecular interactionen
dc.subjectFerric Compoundsen
dc.subjectoxidation reduction reactionen
dc.subjectOxidation-Reductionen
dc.subjectoxygenen
dc.subjectBiological Transporten
dc.subjectcopperen
dc.subjectcatalysisen
dc.subjectquantum mechanicsen
dc.subjecthydrogen bonden
dc.subjectelectron transporten
dc.subjectMolecular Structureen
dc.subjectmolecular dynamicsen
dc.subjectBacterial Proteinsen
dc.subjectProtein Conformationen
dc.subjectprotonen
dc.subjectproton transporten
dc.subjectBinding Sitesen
dc.subjectModels, Molecularen
dc.subjectModels, Chemicalen
dc.subjectProtonsen
dc.subjectRaman spectrometryen
dc.subjectResonance Raman spectroscopyen
dc.subjecthemeen
dc.subjectSpectrum Analysis, Ramanen
dc.subjectvibrationen
dc.subjectElectron Transport Complex IVen
dc.subjectcytochrome c oxidaseen
dc.subjectoxidoreductaseen
dc.subjectHeme-copper oxidaseen
dc.subjectHistidineen
dc.subjectBacillus subtilisen
dc.subjectFerryl intermediateen
dc.subjectheme copper oxidoreductaseen
dc.subjecthydrogen peroxideen
dc.subjectMolecular dynamics simulationen
dc.subjectpropionic aciden
dc.titleThe origin of the Fe IV = O intermediates in cytochrome aa 3 oxidaseen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1016/j.bbabio.2011.07.009
dc.description.volume1817
dc.description.issue4
dc.description.startingpage552
dc.description.endingpage557
dc.author.faculty002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Χημείας / Department of Chemistry
dc.type.uhtypeArticleen
dc.description.notes<p>Cited By :4</p>en
dc.source.abbreviationBiochim.Biophys.Acta Bioenerg.en
dc.contributor.orcidPinakoulaki, Eftychia [0000-0003-3320-6112]
dc.contributor.orcidDaskalakis, Vangelis [0000-0001-8870-0850]
dc.contributor.orcidVarotsis, Constantinos [0000-0003-2771-8891]


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