Investigation of the nature of enzyme-coenzyme interactions in binary and ternary complexes of liver alcohol dehydrogenase with coenzymes, coenzyme analogs, and substrate analogs by ultraviolet absorption and phosphorescence spectroscopy
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00517a022
Reference31 articles.
1. Fluorescence Quenching and Energy Transfer in Complexes between Horse-Liver Alcohol Dehydrogenase and Coenzymes
2. A Fluorescent Analog of Nicotinamide Adenine Dinucleotide
3. Coenzyme-Induced Conformational Changes and Subunit Interactions of Liver Alcohol Dehydrogenase
4. 3 Alcohol Dehydrogenases
5. Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase.
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