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Abstract

The first part of this dissertation deals with investigations on the directed evolution of hybrid catalysts. In addition to hybrid catalyst systems that are based on the covalent attachment of transition metal catalysts or organocatalysts to the host protein, a novel enantioselective hybrid catalyst is describe which is based on an artificial copper(II) binding-site in the host protein.
In the second part, a promiscuous enzymatic activity is described. It is shown that this is the first example of a promiscuous activity that is located outside the natural active site of an enzyme.
The third part describes a novel light-driven direct cofactor regeneration system for flavin-dependent enzymes and evaluates it for a monooxygenase and a reductase.
The final chapter deals with the determination of the substrate scope of YqjM, a reductase from Bacillus subtilis. Furthermore, the development of a platform for the directed evolution of this enzyme is described.