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Cd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation

โœ Scribed by Hemmingsen, L.; Bauer, R.; Bjerrum, M. J.; Zeppezauer, M.; Adolph, H. W.; Formicka, G.; Cedergren-Zeppezauer, E.


Book ID
126141363
Publisher
American Chemical Society
Year
1995
Tongue
English
Weight
1023 KB
Volume
34
Category
Article
ISSN
0006-2960

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Active site substituted Cd(II) horse liver alcohol dehydrogenase has been studied by Perturbed Angular Correlation of Gamma rays Spectroscopy during turnover conditions for benzaldehyde and 4-trans-(N,Ndimethylamino)cinnamaldehyde. The ternary complex between alcohol dehydrogenase NAD + and CI-, and