Characterization of nickel(II) bovine carbonic anhydrase and its inhibitor derivatives
β Scribed by I. Bertini; E. Borghi; C. Luchinat
- Publisher
- Elsevier Science
- Year
- 1978
- Weight
- 589 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0006-3061
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β¦ Synopsis
The nickel(II) derivative of carbonic anhydrase and its adducts with inhii itors have been investigated through electronic and nuclear magnetic resonance (mnrj spectroscopy. The metal ion in the pure enzyme is six-coordinated, and the* is evidence for at least one water molecule in the coordination sphere. Inhibitors replace the water molecule, stiII giving rise to six;coordinated adducts. The affinity of the iuhi%itors is decreased at alkaline pi-I blit &ot be related to a single ionization in the active site cavity.
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π SIMILAR VOLUMES
A Caged Hydrophobic Inhibitor of Carbonic Anhydrase II. -A hydrophobic inhibitor of carbonic anhydrase II, containing an o-nitrophenylglycine protecting group at the sulfonamide moiety, is prepared by standard methods. This caged inhibitor is water-soluble but undergoes deprotection under the activa