Deuterium oxide resonance spectroscopy

It has been proved by X-ray analysis that, in the solid state, 1 is the tautomer present, but the claim has been made that,68 in solution, L-ascorbic acid exists as 2. Structures 3,4, and 5 were readily eliminated by a study of the l3C-n.m.r. spectrum,88,87 and, on the basis of the chemical shifts of the carbon resonances for C-l, C-2, and C-3, and the known chemistry of L-ascorbic acid, 1 is favored over 2 in solution. Berger98 claimed that the proton-carbon-coupled spectrum of L-ascorbic acid is consistent only with structure 1. Ogawa and coworkers87 studied the conformation of L-ascorbic acid and L-ascorbic acid-5-d in deuterium oxide by 13C-n.m.r. spectroscopy, and concluded that, in... 

R. M. Smith, O. Chienthavorn, I. D. Wilson, and B. Wright, Superheated deuterium oxide reversed-phase chromatography coupled to proton nuclear magnetic resonance spectroscopy, Anal. Commun. 35 (1998), 261-263. 

S. Saha, R. M. Smith, E. Lenz, and I. D. Wilson, Analysis of a ginger extract by high-performance liquid chromatography coupled to nuclear magnetic resonance spectroscopy using superheated deuterium oxide as the mobile phase, J. Chromatogr. A 991 (2003), 143-150. 

The assignment of these isomers was confirmed by nuclear magnetic resonance spectroscopy on a Perkin-Elmer 60 Mc./sec. NMR spectrometer, after removal of -OH by exchange with deuterium oxide. The spectrum of the cw-alcohol showed a single broad peak, while that of the trans-alcohol showed two peaks they thus resembled the spectra of the corresponding hydrocarbons (8). 

Nuclear magnetic resonance spectroscopy may provide a convenient measure of the formaldehyde or formic acid produced in some periodate oxidations, and may also permit differentiation between free formic acid and that bound as formic esters deuterium oxide is a convenient solvent for these determinations. Mechanical, automated techniques for determining the amounts of various oxidation products have been developed. ... 

The influence of the protein component of cytochrome c on the haem has also been investigated with the new technique of Raman difference spectroscopy. The basis of the method is similar to conventional difference spectroscopy and the resolution of the haem resonance has been increased S-fold. The method has also been used to study structural changes in methaemoglobin. Williams et a/. have used numerical methods to produce and interpret Raman difference spectra. These workers subtracted solvent spectra from protein spectra and showed that the amide I Raman scattering intensity could be used to define helix, sheet, and reverse turns with unparalleled accuracy. The method depends on computing reference spectra for each variety of secondary structure and fitting these in linear combination to the observed spectrum. The same technique has also been successfully applied to the amide III spectrum of proteins in deuterium oxide. ... 

---