| Abstract
| - The catalytic mechanism for the conversion of carbon dioxide to hydrogen carbonate by acadmium containing carbonic anhydrase was explored at density functional level employing two differentmodels to simulate the active center of the enzyme. In the first model, the histidine residues around themetal ion were replaced with imidazole groups. Instead, in the second one, the simplest model was extendedintroducing two amino acidic residues generally present in the neighbor of enzyme and a deep watermolecule. The results showed that cadmium carbonic anhydrase follows a reaction mechanism that isfavored thermodynamically but not kinetically with respect to that of the most usual zinc-containing enzyme,both in a vacuum and in a protein environment.
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