UCLA

Protein design is a challenging endeavor that attempts to harness the power of nature and engineer it to a particular task. The use of a protein enzyme over a catalyst has both economical and environmental advantages. Discussed here are the initial steps and groundwork in redesigning a metallo-enzyme with the purpose of catalyzing an intramolecular hydroarylation of a carbon-carbon triple bond in the formation of a coumarin. The initial structure scaffold was chosen by comparing structures in the Protein Database. The chosen starting protein, pdb code 1UDV, will be investigated to determine if mutations are necessary to ensure binding of palladium which is the catalyst for the coumarin formation, and folding of the protein. Palladium will be inserted into the active site of the protein and the protein stability will be compared to the corresponding native structure using ΔΔG as a metric. Experimental results will confirm the binding of palladium to the protein and the catalytic efficiency of the enzyme.