The Catalytic Mechanism of Protein Phosphatase 5 Established by DFT Calculations

• Type: Article in International Scientific Journal
• Date: 2013

Authors

Ribeiro, AJ (Author) Other; Alberto, ME (Author) Other; Ramos, MJ (Author) FCUP; Fernandes, PA (Author) FCUP; Russo, N (Author) Other

Journal

Title: Chemistry - A European Journal

Vol. 19

Pages: 14081-14089

ISSN: 0947-6539

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 43 Citations

Scopus - 44 Citations

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9