Zerofield deuterium NMR studies of moderate and strong hydrogen bonds in basic biochemical components and inorganic alkali metal acid salts

Hydrogen bonding occurs when a single atom of hydrogen is shared between two or more electronegative centers. This phenomenon is of central importance in chemistry and biology. Information about the electronic structure in such bonds may be obtained by observing zerofield deuterium NMR spectra. This dissertation concerns zerofield deuterium NMR spectra of moderate and strong hydrogen bonds in basic biochemical components and inorganic alkali metal acid salts. Chapter 4 deals with strong hydrogen bonding in four imidazolium and 1-methylimidazolium salts containing P=O moieties. These inorganic salts play a role in modeling hydrogen bonding in histidine\u27s function as an initiator in enzymatic reactions. Chapter 5 discusses intricate hydrogen bonding in adenosine, guanosine, and inosine. The chapter reports assignments in spectra of anhydrous adenosine in which labile sites are deuterated. Chapter 6 deals with strong hydrogen bonds found in three alkali metal acid salts: sodium deuteron bis-acetate; potassium deuteron bis-acetate; and 70% deuterated cesium chloride$\cdot$1/3(hydronium hydrogen bichloride). These compounds show unusually depressed deuterium quadrupole coupling constants. The first two salts show coupling constants which increase in magnitude upon temperature increase. Chapter 6 discusses this behavior in terms of the vibrational distortions of the hydrogen bonds