The generation of semi-synthetic metalloenzymes has been an active area of study for the past several decades. In order to modify synthetic complexes into water soluble and environmentally benign catalysts, we have covalently attached several inorganic and organometallic compounds into the active sites of native enzymes through site-specific post-translational modification and site directed mutagenesis. Several of these artificial enzymes are catalytically and redox active in aqueous solution. Unfortunately, examples in the literature of semi-synthetic enzymes that exhibit high turnover number and selectivity are not very common due in part to the inherent complexity of the native protein binding pocket. Herein we describe a unique approach to generate artificial metalloproteins in a simple and efficient matter by generating a tunable protein active site without the use of site-directed mutagenesis.

Simple strategy for the design of artificial metalloproteins

244th National Meeting (2012)

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