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Multinuclear NMR studies of hemoproteins and their model compounds

Thesis/Dissertation ·
OSTI ID:5160645
Nuclear magnetic resonance (NMR) in both solution and solid state has been used to study the active site structure of various hemoproteins, and the nature of the iron-oxygen bond in oxyhemoglobin. The first iron-57 NMR spectra of a metalloprotein, carbonmonoxymyoglobin, has been obtained, yielding the isotropic chemical shift, the anisotropy of the chemical shielding tensor and the rotational correlation time of the protein. The oxygen-17 NMR signals from CO ligands bound to oxygen-transport hemoproteins are much narrower than expected, and the lineshape is non-Lorentzian. The results indicate that the unusual linewidths and lineshapes originate from the multiexponential nature of quadrupolar relaxation outside of the extreme narrowing limit, permitting determinations of the oxygen-17 nuclear quadrupole coupling constants and the rotational correlation time of the proteins.
Research Organization:
Illinois Univ., Urbana, IL (USA)
OSTI ID:
5160645
Country of Publication:
United States
Language:
English