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, Eftychiaen
dc.contributor.authorGemeinhardt, Sabineen
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΠινακουλάκη, Ευτυχίαen
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.issued2002en
dc.identifier.citationJournal of biological chemistry, 2002, Volume 277, Issue 26, Pages 23407-23413en
dc.identifier.issn00219258en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6636en
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
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.rights© 2002 by The American Society for Biochemistry and Molecular Biology, Incen
dc.subjectBiochemistryen
dc.subjectLigandsen
dc.subjectDeuteriumen
dc.subjectEnzymesen
dc.subjectNitrogen oxidesen
dc.subjectPhotodissociationen
dc.subjectPhotochemistryen
dc.subjectRaman spectroscopyen
dc.titleNitric-oxide reductase: structure and properties of the catalytic site from resonance Raman scatteringen
dc.typeArticleen
dc.affiliationUniversity of Creteen
dc.identifier.doi10.1074/jbc.M201913200en
dc.dept.handle123456789/54en
item.grantfulltextnone-
item.fulltextNo Fulltext-
item.languageiso639-1other-
crisitem.author.deptDepartment of Environmental Science and Technology-
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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