The Catalytic Mechanism of Protein Phosphatase 5 Established by DFT Calculations

• Tipo: Artigo em Revista Científica Internacional
• Data: 2013

Autores

Ribeiro, AJ (Autor) Outra; Alberto, ME (Autor) Outra; Ramos, MJ (Autor) FCUP; Fernandes, PA (Autor) FCUP; Russo, N (Autor) Outra

Revista

Título: Chemistry - A European Journal

Vol. 19

Páginas: 14081-14089

ISSN: 0947-6539

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 41 Citações

Scopus - 43 Citações

Outras Informações

ID Authenticus: P-006-6KQ

DOI: 10.1002/chem.201301565

Abstract (EN): In order to elucidate the catalytic mechanism of the Mn-Mn containing serine/threonine protein phosphatase5 (PP5), we present a density functional theory study with a cluster model approach. According to our results, the reaction occurs through an in-line concerted transition state with an energy of 15.8kcalmol(-1), and no intermediates are formed. The important role played by His304 and Asp274 as stabilizers of the leaving group has been shown, whereas the role played by the metal ions seems to be mostly electrostatic. The indispensable requirement of having a neutral active center has been demonstrated by testing different protonation states of the cluster model. We have shown also the importance of describing properly the electronic configuration of the Mn-Mn binuclear centers.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 9