Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6636
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dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorGemeinhardt, Sabine-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΠινακουλάκη, Ευτυχία-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T13:40:05Zen
dc.date.accessioned2013-05-16T06:25:23Z-
dc.date.accessioned2015-12-02T10:21:14Z-
dc.date.available2013-01-21T13:40:05Zen
dc.date.available2013-05-16T06:25:23Z-
dc.date.available2015-12-02T10:21:14Z-
dc.date.issued2002-02-26-
dc.identifier.citationJournal of biological chemistry, 2002, vol. 277, no. 26, pp. 23407-23413en_US
dc.identifier.issn0021-9258-
dc.description.abstractWe have applied resonance Raman spectroscopy to investigate the properties of the dinuclear center of oxidized, reduced, and NO-bound nitric-oxide reductase from Paracoccus denitrificans. The spectra of the oxidized enzyme show two distinct vas(Fe-O-Fe) modes at 815 and 833 cm-1 of the heme/non-heme diiron center. The splitting of the Fe-O-Fe mode suggests that two different conformations (open and closed) are present in the catalytic site of the enzyme. We find evidence from deuterium exchange experiments that in the dominant conformation (833 cm-1 mode, closed), the Fe-O-Fe unit is hydrogen-bonded to distal residue(s). The ferric nitrosyl complex of nitric-oxide reductase exhibits the v(Fe3+-NO) and v(N-O) at 594 and 1904 cm-1, respectively. The nitrosyl species we detect is photolabile and can be photolyzed to generate a new form of oxidized enzyme in which the proximal histidine is ligated to heme b3, in contrast to the resting form. Photodissociation of the NO ligand yields a five-coordinate high-spin heme b3. Based on the findings reported here, the structure and properties of the dinuclear center of nitricoxide reductase in the oxidized, reduced, and NO-bound form as well as its photoproduct can be described with certaintyen_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rights© The 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.subjectDeuteriumen_US
dc.subjectEnzymesen_US
dc.subjectNitrogen oxidesen_US
dc.subjectPhotodissociationen_US
dc.subjectPhotochemistryen_US
dc.subjectRaman spectroscopyen_US
dc.titleNitric-oxide reductase: structure and properties of the catalytic site from resonance Raman scatteringen_US
dc.typeArticleen_US
dc.affiliationUniversity of Creteen
dc.collaborationUniversity of Creteen_US
dc.collaborationEuropean Molecular Biology Laboratoryen_US
dc.subject.categoryNATURAL SCIENCESen_US
dc.journalsHybrid Open Accessen_US
dc.countryCyprusen_US
dc.subject.fieldNatural Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1074/jbc.M201913200en_US
dc.dept.handle123456789/54en
dc.relation.issue26en_US
dc.relation.volume277en_US
cut.common.academicyear2002-2003en_US
dc.identifier.spage23407en_US
dc.identifier.epage23413en_US
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextnone-
crisitem.journal.journalissn1083-351X-
crisitem.journal.publisherAmerican Society for Biochemistry and Molecular Biology-
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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