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/20.500.14279/1584
DC FieldValueLanguage
dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorVamvouka, Magdalini-
dc.contributor.authorVarotsis, Constantinos-
dc.date.accessioned2013-01-21T08:30:16Zen
dc.date.accessioned2013-05-16T06:25:21Z-
dc.date.accessioned2015-12-02T10:01:04Z-
dc.date.available2013-01-21T08:30:16Zen
dc.date.available2013-05-16T06:25:21Z-
dc.date.available2015-12-02T10:01:04Z-
dc.date.issued2004-07-08-
dc.identifier.citationInorganic chemistry, 2004, vol. 43, no. 16, pp. 4907-4910en_US
dc.identifier.issn00201669-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/1584-
dc.description.abstractResonance Raman spectroscopy has been employed to investigate the reduced cyano complexes of cytochrome aa3 from bovine heart and Rhodobacter sphaeroides and of cytochrome bo3 from E. coli. In the aa 3-type oxidases, the frequency of the Fe-CN stretching mode is located at 468 cm-1, and the bending Fe-C-N vibration, at 500 cm -1. The fully reduced cytochrome bo3-CN complex gives rise to a stretching vibration at 468 cm-1, a bending vibration at 491 cm-1, and a stretching C-N vibration at 2037 cm-1. The observed differences between aa3 and bo3 oxidases in the frequencies of the Fe-C-N group suggest a quantitative difference in the structure of the His-heme a32+/CuB1+ and His-heme o32+/CuB1+ binuclear pockets upon CN- bindingen_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofInorganic Chemistryen_US
dc.rights© American Chemical Societyen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectCopperen_US
dc.subjectHemeen_US
dc.subjectIronen_US
dc.subjectCattleen_US
dc.subjectRaman spectrometryen_US
dc.subjectVibrationen_US
dc.subjectEnzymesen_US
dc.subjectCytochromesen_US
dc.subjectSpectrum analysisen_US
dc.titleResonance Raman detection of the Fe2+-C-N modes in heme-copper oxidases: a probe of the active siteen_US
dc.typeArticleen_US
dc.collaborationUniversity of Creteen_US
dc.subject.categoryENGINEERING AND TECHNOLOGYen_US
dc.journalsSubscriptionen_US
dc.countryGreeceen_US
dc.subject.fieldEngineering and Technologyen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1021/ic035216ren_US
dc.dept.handle123456789/54en
dc.relation.issue16en_US
dc.relation.volume43en_US
cut.common.academicyear2003-2004en_US
dc.identifier.spage4907en_US
dc.identifier.epage4910en_US
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.languageiso639-1en-
crisitem.journal.journalissn1520-510X-
crisitem.journal.publisherAmerican Chemical Society-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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