University of Illinois Urbana-Champaign

Multinuclear NMR studies of zeolites and heme-proteins

Park, Ki Deok

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Description

Title
Multinuclear NMR studies of zeolites and heme-proteins
Author(s)
Park, Ki Deok
Issue Date
1991
Doctoral Committee Chair(s)
Oldfield, Eric
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Physical
Language
eng
Abstract
  • The quadrupolar interaction having an electrostatic origin, reveals itself in a variety of ways in NMR spectroscopy. In solids, where motions are highly restricted, the quadrupolar interaction is anisotropic and orientation dependent. The static and time dependent parts of the quadrupolar interaction play different roles in the nuclear magnetic resonance experiment. The static part dominates spectral lineshapes, while the latter is revealed in relaxation behavior. In solution, where fast rotational motion exists, the static part of the quadrupolar interaction averages out to zero, while the time dependent part controls spin-lattice relaxation. In this Thesis, two seemingly completely different systems, zeolites in the solid state and proteins in solution, are investigated, using primarily $\sp{17}$O NMR spectroscopy.
  • Chapter 1 is a brief introduction to the origin of the nuclear quadrupolar interaction. In Chapter 2, the temperature dependent nuclear magnetic resonance spin lattice relaxation times of several non-integral spin quadrupolar nuclei ($\sp{17}$O, $\sp{23}$Na, $\sp{27}$Al and $\sp{71}$Ga) in a series of hydrated zeolites (NaA, NaX, NaY, NaGaY, ALPO$\sb4$-5, and NH$\sb4$-ZSM5) at 8.45 Tesla are investigated. In Chapter 3, the oxygen-17 labelling of zeolites ZSM-5, and silica, using $\sp{17}$O$\sb2$ gas, is described, which was a part of an investigation into a series of oxide materials (including Tl$\sb2$O$\sb3$, Bi$\sb2$O$\sb3$, Y$\sb2$O$\sb3$, and BaO$\sb2$). In Chapter 4, distal and proximal-ligand interactions in (C$\sp{17}$O) and ($\sp{13}$CO) -labelled heme proteins are studied. Correlations between C-O and Fe-C vibrational frequencies, oxygen-17 and carbon-13 nuclear magnetic resonance chemical shifts and oxygen-17 nuclear quadrupole coupling constants in (C$\sp{17}$O) and ($\sp{13}$CO) -labelled species are shown and explained in terms of backbonding, and a charge field model.
Type of Resource
text
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Copyright and License Information
Copyright 1991 Park, Ki Deok

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Graduate Dissertations and Theses at Illinois PRIMARY
Graduate Theses and Dissertations at Illinois
Dissertations and Theses - Chemistry