The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenase

1987 ◽  
Vol 14 (7) ◽  
Author(s):  
I. Bertini ◽  
G. Lanini ◽  
C. Luchinat ◽  
C. Haas ◽  
W. Maret ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Metal Ion ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Catalytic Metal

Reactivation of apo horse liver alcohol dehydrogenase with the monovalent metal ion Ag(I)

1982 ◽  
Vol 2 (7) ◽  
pp. 509-514 ◽  
Author(s):  
Lars Skjeldal ◽  
Knut H. Dahl ◽  
John S. McKinley-McKee
Keyword(s):  
Alcohol Dehydrogenase ◽  
Metal Binding ◽  
Metal Ion ◽  
Specific Activity ◽  
Native Enzyme ◽  
Catalytic Center ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Affinity Labelling ◽  
Catalytic Metal

Each subunit of the liver alcohol dehydrogenase dimer contains one catalytic and one structural Zn(II) atom. Enzyme with the catalytic metal atoms selectively removed is inactive but can be partly reactivated in the presence of Ag(I) ions. Reactivation results from Ag(1) ions entering the empty metal-binding site in the catalytic center. The specific activity of this silver enzyme reached 24% of the native enzyme. Atomic absorption analysis gave equal amounts of Ag(I) and Zn(II), corresponding to one mole of each metal per monomer. Metal-directed affinity labelling using bromo-imidazolyl propionate showed that the properties of the silver-reactivated enzyme were distinct from those of the native enzyme.

Sign in / Sign up

Export Citation Format

Share Document