Quenching of the intrinsic fluorescence of liver alcohol dehydrogenase by the alkaline transition and by coenzyme binding
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00369a043
Reference26 articles.
1. Fluorescence Quenching and Energy Transfer in Complexes between Horse-Liver Alcohol Dehydrogenase and Coenzymes
2. Properties of bound trifluoroethanol complexes with horse liver alcohol dehydrogenase
3. Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(2+) and cobalt(2+) ions
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1. Deprotonation of the Horse Liver Alcohol Dehydrogenase−NAD+ Complex Controls Formation of the Ternary Complexes;Biochemistry;2005-09-01
2. Activation of Horse Liver Alcohol Dehydrogenase upon Substitution of Tryptophan 314 at the Dimer Interface;Archives of Biochemistry and Biophysics;1998-10
3. Fourier Transform Infrared Spectroscopic Studies of Proton Transfer Processes and the Dissociation of Zn2+-Bound Water in Alcohol Dehydrogenases;European Journal of Biochemistry;1997-08
4. Tryptophan fluorescence quenching by alkaline pH and ternary complex formation in human β1β1and horse EE alcohol dehydrogenases;FEBS Letters;1992-04-06
5. The pH variation of steady-state kinetic parameters of site-specific Co(2+)-reconstituted liver alcohol dehydrogenase. A mechanistic probe for the assignment of metal-linked ionizations.;Journal of Biological Chemistry;1991-11
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