In this study, theoretical and computational approaches have been utilized to investigate the mechanisms of natural and artificial metalloproteases. The active sites of most natural metalloproteases contain a tetrahedral zinc center, coordinated by three amino acid residues combinated from His(N), Cys(S), Glu(O), and Asp(O) with a water molecule as the fourth ligand. However, the roles played by the ligands environment in the catalytic functions of enzyme are not clear. In this study, the effects of different ligand combinations (NS2, N2S, N2O, N3, S3, NO2 and NSO) in the mechanism were investigated energy barriers were compared. The machanism and energetics of the substrate bound artificial metalloproteases Ni(II)cyclen (cyclen: 1,4,7,10-tetraazacyclododecane) and Cd(II)cyclen have been investigated. In addition, the mechanism of hydrolysis of Phe-Phe peptide bond catalyzed by another artificial metalloprotease [Pd(H2O)4]2+ has also been studied.
| Identifer | oai:union.ndltd.org:UMIAMI/oai:scholarlyrepository.miami.edu:oa_theses-1268 |
| Date | 22 June 2011 |
| Creators | Li, Shanghao |
| Publisher | Scholarly Repository |
| Source Sets | University of Miami |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Open Access Theses |
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