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Πεδίο DCΤιμήΓλώσσα
dc.contributor.authorNicolaides, Antonis-
dc.contributor.authorSoulimane, Tewfik-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΝικολαϊδης, Αντώνης-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.date.accessioned2017-02-01T15:25:16Z-
dc.date.available2017-02-01T15:25:16Z-
dc.date.issued2016-09-01-
dc.identifier.citationBiochimica et Biophysica Acta - Bioenergetics, 2016, vol. 1857, no. 9, pp. 1534-1540en_US
dc.identifier.issn18792650-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/9373-
dc.description.abstractNanosecond time-resolved step-scan FTIR spectroscopy (nTRS 2 -FTIR) has been applied to literally probe the active site of the carbon monoxide (CO)-bound thermophilic ba3 heme-copper oxidoreductase as it executes its function. The nTRS 2 - snapshots of the photolysed heme a3 Fe-CO/CuB species captured a "transition state" whose side chains prevent the photolysed CO to enter the docking cavity. There are three sets of ba3 photoproduct bands of docked CO with different orientation exhibiting different kinetics. The trajectories of the "docked" CO at 2122, 2129 and 2137 cm- 1 is referred to in the literature as B2, B1 and B0 intermediate states, respectively. The present data provided direct evidence for the role of water in controlling ligand orientation in an intracavity protein environment.en_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Bioenergeticsen_US
dc.rights© Elsevieren_US
dc.subjectCytochrome c oxidaseen_US
dc.subjectDynamicsen_US
dc.subjectTime-resolved step-scan FTIRen_US
dc.titleNanosecond ligand migration and functional protein relaxation in ba3 oxidoreductase: Structures of the B0, B1 and B2 intermediate statesen_US
dc.typeArticleen_US
dc.collaborationCyprus University of Technologyen_US
dc.collaborationUniversity of Limericken_US
dc.subject.categoryEarth and Related Environmental Sciencesen_US
dc.journalsOpen Accessen_US
dc.countryCyprusen_US
dc.countryIrelanden_US
dc.subject.fieldNatural Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1016/j.bbabio.2016.05.002en_US
dc.relation.issue9en_US
dc.relation.volume1857en_US
cut.common.academicyear2016-2017en_US
dc.identifier.spage1534en_US
dc.identifier.epage1540en_US
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.cerifentitytypePublications-
item.openairetypearticle-
crisitem.journal.journalissn0005-2728-
crisitem.journal.publisherElsevier-
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.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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