1. Ktisis Cyprus University of Technology
  2. Cyprus University of Technology (Research Output)
  3. Άρθρα/Articles
Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/2209
DC FieldValueLanguage
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorStavrakis, Stavros-
dc.contributor.authorDaskalakis, Vangelis-
dc.contributor.authorVarotsis, Constantinos-
dc.date.accessioned2013-01-21T08:45:18Zen
dc.date.accessioned2013-05-16T06:25:25Z-
dc.date.accessioned2015-12-02T09:15:21Z-
dc.date.available2013-01-21T08:45:18Zen
dc.date.available2013-05-16T06:25:25Z-
dc.date.available2015-12-02T09:15:21Z-
dc.date.issued2004-04-12-
dc.identifier.citationBiochimica et Biophysica Acta - Bioenergetics, 2004, Volume 1655, Issue 1-3, Pages 347-352en_US
dc.identifier.issn52728-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/2209-
dc.description.abstractWe have applied FTIR and time-resolved step-scan Fourier transform infrared (TRS 2-FTIR) spectroscopy to investigate the dynamics of the heme-Cu B binuclear center and the protein dynamics of mammalian aa 3, Pseudomonas stutzeri cbb 3, and caa 3 and ba 3from Thermus thermophilus cytochrome oxidases. The implications of these results with respect to (1) the molecular motions that are general to the photodynamics of the binuclear center in heme-copper oxidases, and (2) the proton pathways located in the ring A propionate of heme a 3-Asp372- H 2O site that is conserved among all structurally known oxidases are discusseden_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Bioenergeticsen_US
dc.rights© 2004 Elsevier B.V. All rights reserveden_US
dc.subjectFourier transform infrared spectroscopyen_US
dc.subjectHemeen_US
dc.subjectCopperen_US
dc.subjectMammalsen_US
dc.subjectPseudomonasen_US
dc.subjectOxygenen_US
dc.subjectMolecular dynamicsen_US
dc.titleTime-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: implications for O 2 input and H 2O/H + output channelsen_US
dc.typeArticleen_US
dc.affiliationUniversity of Creteen
dc.collaborationUniversity of Creteen_US
dc.subject.categoryChemical Sciencesen_US
dc.journalsSubscription Journalen_US
dc.countryGreeceen_US
dc.subject.fieldNatural Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1016/j.bbabio.2003.06.004en_US
dc.dept.handle123456789/54en
cut.common.academicyear2004-2005en_US
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.languageiso639-1en-
crisitem.journal.journalissn0005-2728-
crisitem.journal.publisherElsevier-
crisitem.author.deptDepartment of Chemical Engineering-
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.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0001-9301-1021-
crisitem.author.orcid0000-0001-8870-0850-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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