Ein L 3 ZnOH‐Komplex als funktionelles Modell des Enzyms Carboanhydrase
Author:
Affiliation:
1. Institut für Anorganische und Analytische Chemie der Universität Freiburga, Albertstraße 21, W‐7800 Freiburg, F.R.G.
2. Du Pont Polymers, Experimental Station, Building 302/216b, P.O. Box 80302, Wilmington, Delaware, 19880‐0302, U.S.A.
Publisher
Wiley
Subject
Inorganic Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cber.19931260322
Reference41 articles.
1. Binding of substrate CO2 to the active site of human carbonic anhydrase II: a molecular dynamics study.
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3. An ab initio study of transition structures and associated products in [ZnOHCO2]+, [ZnHCO3H2O]+, and [Zn(NH3)3HCO3]+ hypersurfaces. On the role of zinc in the catalytic mechanism of carbonic anhydrase
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