Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/3300
DC FieldValueLanguage
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.authorSoulimane, Tewfik-
dc.contributor.authorVarotsis, Constantinos-
dc.date.accessioned2013-01-16T13:52:28Zen
dc.date.accessioned2013-05-17T07:13:16Z-
dc.date.accessioned2015-12-08T07:52:46Z-
dc.date.available2013-01-16T13:52:28Zen
dc.date.available2013-05-17T07:13:16Z-
dc.date.available2015-12-08T07:52:46Z-
dc.date.issued2012-08-27-
dc.identifier.citationJournal of Biological Chemistry, vol. 287, no. 44, pp. 37495-37507en_US
dc.identifier.issn1083351X-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/3300-
dc.description.abstractBackground: Cytochrome c oxidase reduces O 2 to H 2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba 3-CO does not lead to a heme a 3 3+-Cu B 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a 3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba 3 oxidase are presenteden_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rights© 2012 by The American society for biochemistry and molecular biology, Incen_US
dc.subjectPorphyrinsen_US
dc.subjectPhotochemistryen_US
dc.subjectCytochrome oxidaseen_US
dc.subjectCarbon monoxideen_US
dc.subjectInfrared spectroscopyen_US
dc.subjectThermodynamicsen_US
dc.titleSpectroscopic and Kinetic Investigation of the Fully Reduced and Mixed Valence States of Ba 3-Cytochrome C Oxidase From Hermus Thermophilus a Fourier Transform Infrared (FTIR) and Time-Resolved Step-Scan FTIR Studyen_US
dc.typeArticleen_US
dc.collaborationCyprus University of Technologyen_US
dc.collaborationUniversity of Limericken_US
dc.subject.categoryChemical Sciencesen_US
dc.journalsSubscriptionen_US
dc.countryCyprusen_US
dc.countryIrelanden_US
dc.subject.fieldNatural Sciencesen_US
dc.identifier.doi10.1074/jbc.M112.403600en_US
dc.identifier.pmid22927441-
dc.dept.handle123456789/77en
dc.relation.issue44en_US
dc.relation.volume287en_US
cut.common.academicyear2011-2012en_US
dc.identifier.spage37495en_US
dc.identifier.epage37507en_US
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.languageiso639-1en-
crisitem.journal.journalissn1083-351X-
crisitem.journal.publisherAmerican Society for Biochemistry and Molecular Biology-
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.orcid0000-0001-9301-1021-
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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