In order to elucidate the catalytic mechanism of the Mn-Mn containing serine/threonine protein phosphatase 5 (PP5), we present a density functional theory study with a cluster model approach. According to our results, the reaction occurs through an inline concerted transition state with an energy of 15.8 kcalmol-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.
Ribeiro, A., Alberto, M., Ramos, M., Fernandes, P., Russo, N. (2013). The catalytic mechanism of protein phosphatase 5 established by DFT calculations. CHEMISTRY-A EUROPEAN JOURNAL, 19(42), 14081-14089 [10.1002/chem.201301565].
The catalytic mechanism of protein phosphatase 5 established by DFT calculations
Alberto M. E.;
2013
Abstract
In order to elucidate the catalytic mechanism of the Mn-Mn containing serine/threonine protein phosphatase 5 (PP5), we present a density functional theory study with a cluster model approach. According to our results, the reaction occurs through an inline concerted transition state with an energy of 15.8 kcalmol-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.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
