A quantum-mechanical study of the reaction mechanism of sulfite oxidase
| Autor: | Ebbe Nordlander, Ulf Ryde, Kerstin Starke, Ricardo A. Mata, Marie-Celine Van Severen, Jilai Li, Milica Andrejić |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Reaction mechanism Atom and Molecular Physics and Optics Crystallography X-Ray Biochemistry Inorganic Chemistry chemistry.chemical_compound Sulfite Computational chemistry Sulfite oxidase Theoretical chemistry Animals Sulfites Theoretical Chemistry Molybdenum biology Chemistry Sulfates Sulfite Oxidase Solvation Active site Hybrid functional biology.protein Quantum Theory Density functional theory Chickens Oxidation-Reduction |
| Zdroj: | Journal of Biological Inorganic Chemistry; 19(7), pp 1165-1179 (2014) |
| ISSN: | 1432-1327 |
| Popis: | The oxidation of sulfite to sulfate by two different models of the active site of sulfite oxidase has been studied. Both protonated and deprotonated substrates were tested. Geometries were optimized with density functional theory (TPSS/def2-SV(P)) and energies were calculated either with hybrid functionals and large basis sets (B3LYP/def2-TZVPD) including corrections for dispersion, solvation, and entropy, or with coupled-cluster theory (LCCSD(T0)) extrapolated toward a complete basis set. Three suggested reaction mechanisms have been compared and the results show that the lowest barriers are obtained for a mechanism where the substrate attacks a Mo-bound oxo ligand, directly forming a Mo-bound sulfate complex, which then dissociates into the products. Such a mechanism is more favorable than mechanisms involving a Mo-sulfite complex with the substrate coordinating either by the S or O atom. The activation energy is dominated by the Coulomb repulsion between the Mo complex and the substrate, which both have a negative charge of -1 or -2. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink