title: The working mechanism of the β-carbonic anhydrase degrading carbonyl sulphide (COSase): a theoretical study.
abstract: In order to give insights into the working mechanism of the novel characterized enzyme carbonyl sulphide hydrolase (COSase), which efficiently converts COS into H2S and CO2, we have performed a detailed theoretical investigation using the framework of density functional theory (using B3LYP and M06 exchange-correlation functionals) by the cluster model approach. In the final part of the reaction the metal ion is unable to form a pentacoordinated species. The B3LYP-D3 and M06 potential energy surfaces have a very similar shape. The elucidation of the catalytic reduction of COS is important in view of its role in environmental chemistry.
authors.affiliation: Dipartimento di Chimica e Tecnologie Chimiche, Università della Calabria, Cubo 14C, Via P. Bucci, 87036 Arcavacata di Rende (CS), Italy. tmarino@unical.it.
authors.forename: P
authors.initials: P
authors.lastname: Piazzetta
authors.forename: T
authors.initials: T
authors.lastname: Marino
authors.forename: N
authors.initials: N
authors.lastname: Russo
mesh_terms: D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000648:ultrastructure*; D002384:Catalysis; D003198:Computer Simulation; D004789:Enzyme Activation; D008956:Models, Chemical; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011789:Quantum Theory; D013440:Sulfides / Q000737:chemistry*
chemical_list: D013440:Sulfides; D002256:Carbonic Anhydrases