Luminescence studies on the conformational behavior of horse-liver alcohol dehydrogenase

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Abstract
The luminescence quenching and conformational behaviour 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 nonradiating energy transfer from Trp-314 to NADH was observed. An essential energy transfer from Trp-15 to NADH and between the two Trp-314 residues of both subunits of the enzyme was not revealed. The quenching of the enzyme luminescence upon NAD+ binding was caused mainly, by NAD+ reduction 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.