Solid-State C-13 Nmr Evidence for a Large Deviation from Linearity of the Fe-C-O Unit in the Co Complex with Myoglobin
| dc.contributor.author | Gerothanassis, I. P. | en |
| dc.contributor.author | Barrie, P. J. | en |
| dc.contributor.author | Momenteau, M. | en |
| dc.contributor.author | Hawkes, G. E. | en |
| dc.date.accessioned | 2015-11-24T16:47:30Z | |
| dc.date.available | 2015-11-24T16:47:30Z | |
| dc.identifier.issn | 0002-7863 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9195 | |
| dc.rights | Default Licence | - |
| dc.subject | nuclear-magnetic-resonance | en |
| dc.subject | carbon-monoxide binding | en |
| dc.subject | sperm whale myoglobin | en |
| dc.subject | heme-proteins | en |
| dc.subject | neutron-diffraction | en |
| dc.subject | ligand-binding | en |
| dc.subject | model compounds | en |
| dc.subject | bond angle | en |
| dc.subject | iron | en |
| dc.subject | spectroscopy | en |
| dc.title | Solid-State C-13 Nmr Evidence for a Large Deviation from Linearity of the Fe-C-O Unit in the Co Complex with Myoglobin | en |
| heal.abstract | The 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.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | <Go to ISI>://A1994QA28800038 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdf/10.1021/ja00105a038 | - |
| heal.journalName | J Am Chem Soc | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1994 | - |
| heal.publisher | American Chemical Society | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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