PMID: 6989599Feb 1, 1980Paper

The peroxidatic reaction catalyed by horse liver alcohol dehydrogenase. 3. Nuclear magnetic resonance spectroscopic study of NADX

European Journal of Biochemistry
A MazziniM A Abdallah

Abstract

As previously reported [Favilla, R. & Cavatorta, P. (1975) FEBS Lett. 50, 324-329], the enzyme horse liver alcohol dehydrogenase catalyzes a reaction between NAD+ and H2O2. The final isolated product was then called NADX because of its unknown structure. In this paper the results of spectroscopic investigations on this compound are described. They indicate that only the nicotinamide moiety of the original NAD+ molecule was modified by the action of hydrogen peroxide. From the 1H and 13C nuclear magnetic resonance spectra of NADX the following structure was deduced: adenosine(5')diphospho(5)-beta-D-ribose-NH-CH = C(CHO)-CONH2. This structure is consistent with both ultraviolet and reactivity measurements performed on NADX. A tentative mechanism for the whole peroxidatic reaction pathway leading to NADX is finally proposed.

Related Concepts

NADX
Adenosine Diphosphate Ribose
Alcohol Oxidoreductases
Oxydol
Liver
In Vivo NMR Spectroscopy
Nucleoside Diphosphate Sugars
Oxidation-Reduction

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