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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Gerothanassis, I. P. | en |
| dc.contributor.author | Momenteau, M. | en |
| dc.contributor.author | Barrie, P. J. | en |
| dc.contributor.author | Kalodimos, C. G. | en |
| dc.contributor.author | Hawkes, G. E. | en |
| dc.date.accessioned | 2015-11-24T16:53:19Z | - |
| dc.date.available | 2015-11-24T16:53:19Z | - |
| dc.identifier.issn | 0020-1669 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10002 | - |
| dc.rights | Default Licence | - |
| dc.subject | resonance raman-spectroscopy | en |
| dc.subject | oxygen-binding hemoproteins | en |
| dc.subject | nuclear-magnetic-resonance | en |
| dc.subject | heme-proteins | en |
| dc.subject | capped porphyrin | en |
| dc.subject | carbon-monoxide | en |
| dc.subject | co binding | en |
| dc.subject | pocket porphyrins | en |
| dc.subject | iron-porphyrins | en |
| dc.subject | chemical-shifts | en |
| dc.title | C-13 CP/MAS NMR studies of hemoprotein models with and without an axial hindered base: C-13 shielding tensors and comparison with hemoproteins and X-ray structural data | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://A1996UH03300040 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdfplus/10.1021/ic950830r | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1996 | - |
| heal.abstract | C-13 cross-polarization magic-angle-spinning (CP/MAS) NMR spectra of several carbonmonoxide (93-99% C-13 enriched) hemoprotein models with 1,2-dimethylimidazole (12-diMeIm) and 1-methylimidazole (1-MeIm) as axial ligands are reported. This enables the (CO)-C-13 spinning sideband manifold to be measured and hence the principal components of the (CO)-C-13 chemical shift tensor to be obtained. Negative polar interactions in the binding pocket of the cap porphyrin model and inhibition of Fe-->CO back-donation result in a reduction in shielding anisotropy; on the contrary, positive distal polar interactions result in an increase in the shielding anisotropy and asymmetry parameter in some models. It appears that the axial hindered base 1,2-dimethylimidazole has little direct effect on the local geometry at the CO site, despite higher rates of CO desorption being observed for such complexes. This suggests that the mechanism by which steric interactions are released for the 1,2-diMeIm complexes compared to 1-MeIm complexes does not involve a significant increase in bending of the Fe-C-O unit. The asymmetry of the shielding tensor of all the heme model compounds studied is smaller than that found for horse myoglobin and rabbit hemoglobin. | en |
| heal.publisher | American Chemical Society | en |
| heal.journalName | Inorg Chem | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Gerothanassis-1996-C-13 CP_MAS NMR stud.pdf | 279.46 kB | Adobe PDF | View/Open Request a copy |
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