Structural Differences of the Iron Dioxygen Moiety of Hemoprotein Models with and without an Axial Hindered Base as Revealed by O-17 Nmr and Ftir Spectroscopy in Solution

dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorLoock, B.en
dc.contributor.authorMomenteau, M.en
dc.date.accessioned2015-11-24T16:48:04Z
dc.date.available2015-11-24T16:48:04Z
dc.identifier.issn0022-4936-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9276
dc.rightsDefault Licence-
dc.subjecthemoglobin cooperativityen
dc.subjectoxygen-bindingen
dc.subjectcarbon-monoxideen
dc.subjectt-stateen
dc.subjectporphyrinsen
dc.subjectbonden
dc.subjecthemoproteinsen
dc.subjectcoordinationen
dc.subjectsystemsen
dc.titleStructural Differences of the Iron Dioxygen Moiety of Hemoprotein Models with and without an Axial Hindered Base as Revealed by O-17 Nmr and Ftir Spectroscopy in Solutionen
heal.abstractThe N-H stretching vibrations of the oxygenated 'hybrid' haemoprotein models with an axial hindered base indicate that there is no conventional hydrogen bond with the terminal oxygen of the Fe-O2 moiety, contrary to the models with an axial unhindered base; however, the Fe-O2 moiety is highly polarizable as indicated by O-17 NMR spectroscopy.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDoi 10.1039/C39920000598-
heal.identifier.secondary<Go to ISI>://A1992HQ25100006-
heal.identifier.secondaryhttp://pubs.rsc.org/en/Content/ArticleLanding/1992/C3/c39920000598-
heal.journalNameJournal of the Chemical Society-Chemical Communicationsen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1992-
heal.publisherRoyal Society of Chemistryen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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