Flexibility of a biotinylated ligand in artificial metalloenzymes based on streptavidin--an insight from molecular dynamics simulations with classical and ab initio force fields.

ABSTRACT: In the field of enzymatic catalysis, creating activity from a non catalytic scaffold is a daunting task. Introduction of a catalytically active moiety within a protein scaffold offers an attractive means for the creation of artificial metalloenzymes. With this goal in mind, introduction of a biotinylated d(6)-piano-stool complex within streptavidin (SAV) affords enantioselective artificial transfer-hydrogenases for the reduction of prochiral ketones. Based on an X-ray crystal structure of a highly selective hybrid catalyst, displaying significant disorder around the biotinylated catalyst [eta(6)-(p-cymene)Ru(Biot-p-L)Cl], we report on molecular dynamics simulations to shed light on the protein-cofactor interactions and contacts. The results of these simulations with classical force field i

SUBMITTER: Panek JJ 

PROVIDER: S-EPMC2918797 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature