Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/1778
DC FieldValueLanguage
dc.contributor.authorStavrakis, Stavros-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.otherΣταυράκης, Σταύρος-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.contributor.otherΚουτσουπάκης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T13:41:05Zen
dc.date.accessioned2013-05-16T06:25:14Z-
dc.date.accessioned2015-12-02T09:45:32Z-
dc.date.available2013-01-21T13:41:05Zen
dc.date.available2013-05-16T06:25:14Z-
dc.date.available2015-12-02T09:45:32Z-
dc.date.issued2002-09-06-
dc.identifier.citationJournal of biological chemistry, 2002, vol. 277, no. 36, pp. 32860-32866en_US
dc.identifier.issn00219258-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/1778-
dc.description.abstractWe report the first evidence for the existence of the equilibrium Cu B 1+-CO species of CO-bound reduced cytochrome ba 3 from Thermus thermophilus at room temperature. The frequency of the C-O stretching mode of Cu B 1+-CO is located at 2053 cm -1 and remains unchanged in H 2O/D 2O exchanges and, between pD 5.5 and 9.7, indicating that the chemical environment does not alter the protonation state of the Cu B histidine ligands. The data and conclusions reported here are in contrast to the changes in protonation state of Cu B-His-290, reported recently (Das, T. K., Tomson, F. K., Gennis, R. B., Gordon, M., and Rousseau, D. L. (2001) Biophys. J. 80, 2039-2045 and Das, T. P., Gomes, C. M., Teixeira, M., and Rousseau, D. L. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 9591-9596). The time-resolved step-scan FTIR difference spectra indicate that the rate of decay of the transient CU B 1+-CO complex is 34.5 s -1 and rebinding to heme a 3 occurs with k 2 = 28.6 s -1. The rate of decay of the transient Cu B 1+-CO complex displays a similar time constant as the absorption changes at 1694(+)/1706(-), attributed to perturbation of the heme a 3 propionates (COOH). The ν(C-O) of the transient Cu B 1+-CO species is the same as that of the equilibrium Cu B 1+-CO species and remains unchanged in the pD range 5.5-9.7 indicating that no structural change takes place at Cu B between these states. The implications of these results with respect to proton pathways in heme-copper oxidases are discusseden_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rights© American Society for Biochemistry and Molecular Biologyen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectBiochemistryen_US
dc.subjectLigandsen_US
dc.subjectAbsorptionen_US
dc.subjectCopper compoundsen_US
dc.subjectFourier transform infrared spectroscopyen_US
dc.subjectProtonsen_US
dc.subjectCarbonen_US
dc.subjectHistidineen_US
dc.subjectBacteriaen_US
dc.titleObservation of the equilibrium Cu B-CO complex and functional implications of the transient heme a 3 propionates in cytochrome ba 3-CO from Thermus thermophilus. Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studiesen_US
dc.typeArticleen_US
dc.affiliationUniversity of Creteen
dc.collaborationUniversity of Creteen_US
dc.subject.categoryChemical Sciencesen_US
dc.journalsHybrid Open Accessen_US
dc.countryGreeceen_US
dc.subject.fieldNatural Sciencesen_US
dc.identifier.doi10.1074/jbc.M204943200en_US
dc.dept.handle123456789/54en
dc.relation.issue36en_US
dc.relation.volume277en_US
cut.common.academicyear2002-2003en_US
dc.identifier.spage32860en_US
dc.identifier.epage32866en_US
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.cerifentitytypePublications-
item.openairetypearticle-
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.orcid0000-0003-2771-8891-
crisitem.author.orcid0000-0001-9301-1021-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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