| Issue |
J. Phys. Colloques
Volume 47, Number C8, Décembre 1986
EXAFS and Near Edge Structure IV
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|---|---|---|
| Page(s) | C8-1165 - C8-1168 | |
| DOI | https://doi.org/10.1051/jphyscol:19868227 | |
EXAFS and Near Edge Structure IV
J. Phys. Colloques 47 (1986) C8-1165-C8-1168
DOI: 10.1051/jphyscol:19868227
1 Fachbereich 15.2, Analytische und Biologische Chemie, Universität des Saarlandes, D-6600 Saarbrücken, F.R.G.
2 European Molecular Biology Laboratory (EMBL), C/o DESY, Notkestrasse 85, D-2000 Hamburg 52, F.R.G.
J. Phys. Colloques 47 (1986) C8-1165-C8-1168
DOI: 10.1051/jphyscol:19868227
EXAFS INVESTIGATION OF THE STRUCTURAL SITE OF LIVER ALCOHOL DEHYDROGENASE
M. ZEPPEZAUER1, C. HAAS1, W. MARET1, C. HERMES2 et R.F. PETTIFER21 Fachbereich 15.2, Analytische und Biologische Chemie, Universität des Saarlandes, D-6600 Saarbrücken, F.R.G.
2 European Molecular Biology Laboratory (EMBL), C/o DESY, Notkestrasse 85, D-2000 Hamburg 52, F.R.G.
Abstract
Date are presented of the X-ray absorption near edge and EXAFS region for the Zinc environment of the structural site of horse liver alcohol dehydrogenase (HLADH). Using metal replacement or extraction, X-ray absorption measurements could be performed exclusively on the structural site. Measurements were performed at 20 K both on 3 types of enzyme (HLADH without catalytic centres, HLADH with coenzyme and HLADH with inhibitor bound to the active site) and on 2 model compounds namely cubic Zinc sulphide and Zinc dimethyldithiocarbamate. Both, the mean interatomic distance (Zn-S) and the thermal parameters indicate that the enzymes' local structure is most closely modelled by cubic Zinc sulphide.