Ligand Binding to the blue copper center of horse liver alcohol dehydrogenase

The catalytic zinc ion of horse liver alcohol dehydrogenase (LADH) is liganded by 2 thiol groups (Cys 46 and 174) and one imidazole nitrogen (His 67), its fourth ligand being water. Incorporation of Cu super(2+) into the catalytic zinc binding site of horse liver alcohol dehydrogenase (EC 1.1.1.1) p...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 136; no. 1; pp. 72 - 74
Main Authors Maret, W., Zeppezauer, M., Desideri, A., Morpurgo, L., Rotilio, G.
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 21.12.1981
Subjects
alcohol dehydrogenase
Alcohol Oxidoreductases - metabolism
Animals
Anions
Azides - metabolism
Copper
Cyanides - metabolism
E.S.R
Electron Spin Resonance Spectroscopy
Horses
Imidazoles - metabolism
Ligands - metabolism
liver
Liver - enzymology
Spectrophotometry, Ultraviolet
Online AccessGet full text

Cover

More Information
Summary:The catalytic zinc ion of horse liver alcohol dehydrogenase (LADH) is liganded by 2 thiol groups (Cys 46 and 174) and one imidazole nitrogen (His 67), its fourth ligand being water. Incorporation of Cu super(2+) into the catalytic zinc binding site of horse liver alcohol dehydrogenase (EC 1.1.1.1) produces a metastable cupric protein. Here, the authors describe results of EPR and optical absorption spectroscopy studies of several complexes of Cu-LADH with small anionic ligand molecules, such as cyanide, azide, imidazole and 2-mercaptoethanol. These complexes were found to be metastable and their EPR spectra were indicative of a geometry more tetragonal than in the unliganded cupric enzyme. Binding of NAD super(+) and NADH to the cupric enzyme gave rise to EPR spectra similar to those observed in "blue" copper centers.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(81)81216-1