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dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorBarrie, P. J.en
dc.contributor.authorMomenteau, M.en
dc.contributor.authorHawkes, G. E.en
dc.date.accessioned2015-11-24T16:47:30Z-
dc.date.available2015-11-24T16:47:30Z-
dc.identifier.issn0002-7863-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9195-
dc.rightsDefault Licence-
dc.subjectnuclear-magnetic-resonanceen
dc.subjectcarbon-monoxide bindingen
dc.subjectsperm whale myoglobinen
dc.subjectheme-proteinsen
dc.subjectneutron-diffractionen
dc.subjectligand-bindingen
dc.subjectmodel compoundsen
dc.subjectbond angleen
dc.subjectironen
dc.subjectspectroscopyen
dc.titleSolid-State C-13 Nmr Evidence for a Large Deviation from Linearity of the Fe-C-O Unit in the Co Complex with Myoglobinen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://A1994QA28800038-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdf/10.1021/ja00105a038-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1994-
heal.abstractThe application of high-resolution solid-state C-13 NMR spectroscopy to investigate the bending between carbon monoxide and myoglobin is explored. Selective pulse sequences (non-quaternary suppression and SELDOM) significantly reduce the problem of (CO)-C-13 peaks overlapping with those arising from the natural C-13 abundance myoglobin molecule. This enables the (CO)-C-13 spinning sideband manifold to be measured and, hence, the principal components of the (CO)-C-13 chemical shift tenser to be obtained. Results were obtained on two samples of myoglobin: one a dry powder and the other carefully prepared needle-like crystals containing water of crystallization. The spectra show that there is a large increase in the asymmetry of the C-13 Shielding tenser in (CO)-C-13-myoglobin compared to heme model compounds containing close to linear Fe-C-O moieties. FTIR measurements of both myoglobin samples show that the major nu(co) stretching frequency is due to the A(3) conformer. It can be concluded that in this particular CO-myoglobin substate there must be substantial deviation from linearity of the Fe-C-O unit, probably due to a significant polar interaction with the distal histidine.en
heal.publisherAmerican Chemical Societyen
heal.journalNameJ Am Chem Socen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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