A carbon-13 NMR comparative study of metal ion substitutions in human carbonic anhydrase I carboxymethylated at active-site Histidine-200
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference36 articles.
1. Investigation of the system carbon dioxide-bicarbonate(1-) ion in the presence of copper(II) bovine carbonic anhydrase B
2. Hydrogen-Exchange Study of the Conformational Stability of Human Carbonic-Anhydrase B and Its Metallocomplexes
3. Water in the coordination sphere of metallocarbonic anhydrases: A solvent proton longitudinal relaxation study at several frequencies
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1. Interaction of the unique competitive inhibitor imidazole and related compounds with the active site metal of carbonic anhydrase: linkage between pH effects on the inhibitor binding affinity and pH effects on the visible spectra of inhibitor complexes with the cobalt-substituted enzyme;Biochemistry;1987-11-01
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