Electron Paramagnetic Resonance of d-Xylose Isomerase: Evidence for Metal Ion Movement Induced by Binding of Cyclic Substrates and Inhibitors
Author:
Affiliation:
1. Institut für Biochemie, Universität Münster, Wilhelm Klemm Strasse 2, D-48149 Münster, Germany, and Fachrichtung für Biophysik und Physikalische Grundlagen der Medizin, Universität des Saarlandes, D-66421 Homburg (Saar), Germany
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi962406n
Reference33 articles.
1. Visible, EPR and electron nuclear double-resonance spectroscopic studies on the two metal-binding sites of oxovanadium (IV)-substituted D-xylose isomerase
2. X- and Q-band EPR studies on the two Mn2+-substituted metal-binding sites of d-xylose isomerase
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3. L-Arabinose Binding, Isomerization, and Epimerization by D-Xylose Isomerase: X-Ray/Neutron Crystallographic and Molecular Simulation Study;Structure;2014-09
4. Binding Energy and Catalysis by d-Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of (R)-Glyceraldehyde;Biochemistry;2011-10-27
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