title: A comparative study of the catalytic mechanisms of the zinc and cadmium containing carbonic anhydrase.
abstract: The catalytic mechanism for the conversion of carbon dioxide to hydrogen carbonate by a cadmium containing carbonic anhydrase was explored at density functional level employing two different models to simulate the active center of the enzyme. In the first model, the histidine residues around the metal ion were replaced with imidazole groups. Instead, in the second one, the simplest model was extended introducing two amino acidic residues generally present in the neighbor of enzyme and a deep water molecule. The results showed that cadmium carbonic anhydrase follows a reaction mechanism that is favored thermodynamically but not kinetically with respect to that of the most usual zinc-containing enzyme, both in a vacuum and in a protein environment.
authors.affiliation: Dipartimento di Chimica and Centro di Calcolo ad Alte Prestazioni per Elaborazioni Parallele e Distribuite-Centro d'Eccellenza MIUR, Università della Calabria, I-87030 Arcavacata di Rende (CS), Italy.
authors.forename: Tiziana
authors.initials: T
authors.lastname: Marino
authors.forename: Nino
authors.initials: N
authors.lastname: Russo
authors.forename: Marirosa
authors.initials: M
authors.lastname: Toscano
mesh_terms: D002104:Cadmium / Q000737:chemistry* / Q000378:metabolism*; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D008956:Models, Chemical; D008958:Models, Molecular; D013816:Thermodynamics; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002104:Cadmium; D002256:Carbonic Anhydrases; D015032:Zinc