title: [Luminescence study of the conformation behavior of alcohol dehydrogenase from horse liver during substrate binding].
abstract: The luminescence quenching and conformational behavior of alcohol dehydrogenase from horse liver upon substrate binding has been studied. It was shown that the binding of NADH and NAD+ to the enzyme resulted in the quenching of Trp-314 luminescence, whereas the luminescence of Trp-15 was not quenched. In this case non-radiating energy transfer from Trp-314 to NADH was observed. An essential energy transfer from Trp-15 to NADH and between the two Trp-314 of both subunits of the enzyme was not revealed. The quenching of the enzyme luminescence upon NAD+ binding was, mainly, caused by NAD+ reduction up to NADH. It was assumed, that the release of the proton upon NAD+ binding occurred due to the reduction. Binding of ethanol, ADP or adenosine did not result in essential conformational changes of the enzyme.
authors.forename: N L
authors.initials: NL
authors.lastname: Vekshin
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D006736:Horses; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008163:Luminescent Measurements; D009243:NAD / Q000378:metabolism; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
chemical_list: D009243:NAD; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase
vernacular_title: Liuminestsentnoe izuchenie konformatsionnogo povedeniia alkogol'degidrogenazy iz pecheni loshadi pri sviazyvanii substratov.