Low-affinity interaction of ethanol with the fluorescent complex between horse liver alcohol dehydrogenase and auramine O.
Quenching of the fluorescence of the complex between horse liver alcohol dehydrogenase (alcohol:NAD+ oxidoreductase (EC 1.1.1.1) and auramine O complex is inconsistent with a simple competitive displacement of auramine O by ethanol. Instead, the action of ethanol requires an explanation in terms of a solvent effect, or the formation of an enzyme-auramine O-ethanol ternary complex. The latter complex would have to be the low-affinity variety similar to the enzyme-NADH-ethanol ternary complex encountered in the kinetic system.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000814:Aniline Compounds / Q000378:metabolism; D000817:Anilino Naphthalenesulfonates; D000818:Animals; D001576:Benzophenoneidum / Q000378:metabolism; D001665:Binding Sites; D000431:Ethanol; D006736:Horses; D008099:Liver / Q000201:enzymology; D009243:NAD; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D000814:Aniline Compounds; D000817:Anilino Naphthalenesulfonates; D009243:NAD; D001576:Benzophenoneidum; D000431:Ethanol; D000429:Alcohol Oxidoreductases