Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/1551
DC FieldValueLanguage
dc.contributor.authorStavrakis, Stavros-
dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΣταυράκης, Σταύρος-
dc.contributor.otherΠινακουλάκη, Ευτυχία-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T11:33:51Zen
dc.date.accessioned2013-05-16T06:25:13Z-
dc.date.accessioned2015-12-02T10:11:35Z-
dc.date.available2013-01-21T11:33:51Zen
dc.date.available2013-05-16T06:25:13Z-
dc.date.available2015-12-02T10:11:35Z-
dc.date.issued2002-11-21-
dc.identifier.citationJournal of physical chemistry B, 2002, vol. 106, no. 50, pp. 12860-12862en_US
dc.identifier.issn10895647-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/1551-
dc.description.abstractWe report the first vibrational study of NO bound to an oxidized heme-copper oxidase. Cytochrome cbb 3 oxidase from P. stutzeri reduces both O 2 and NO to H 2O and N 2O, respectively. The ferric nitrosyl complex of cbb 3 exhibits v(N-O) at 1903 cm -1. This frequency is very similar to v(NO) of nitric oxide reductase, the acidic form of Met Mb-NO, but 18 cm -1 lower than that of neutral Met Mb-NO. By monitoring the NO intensity, we estimate that NO dissociates from the heme b 3 pocket, without binding to Cu B, with k = 1.8 × 10 -3 s -1. Therefore, NO binding occurs at the heme site and not at Cu B, generating a nitrosonium Cu B 1+-NO + species as proposed recently (Torres; J.; Cooper, C.E.; Wilson, M.T. J. Biol. Chem. 1998, 273, 8756-8766). The coordination of NO to cbb 3 oxidase and to nitric oxide reductase and Mb is compared and discusseden_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofJournal of Physical Chemistry Ben_US
dc.rights© American Chemical Societyen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectFourier transform infrared spectroscopyen_US
dc.subjectOrganometallic chemistryen_US
dc.subjectChemical bondsen_US
dc.subjectDissociationen_US
dc.subjectNitrogen oxidesen_US
dc.subjectOxidationen_US
dc.titleFourier transform infrared evidence for a ferric six-coordinate nitrosylheme b 3 complex of cytochrome cbb 3 oxidase from Pseudomonas stutzeri at ambient temperatureen_US
dc.typeArticleen_US
dc.affiliationUniversity of Creteen
dc.collaborationUniversity of Oklahomaen_US
dc.subject.categoryChemical Sciencesen_US
dc.journalsHybrid Open Accessen_US
dc.countryCyprusen_US
dc.subject.fieldNatural Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1021/jp026763len_US
dc.dept.handle123456789/54en
dc.relation.issue50en_US
dc.relation.volume106en_US
cut.common.academicyear2020-2021en_US
dc.identifier.spage12860en_US
dc.identifier.epage12862en_US
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.fulltextNo Fulltext-
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-
crisitem.journal.journalissn1520-5207-
crisitem.journal.publisherAmerican Chemical Society-
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