- Catalysis for the synthesis of fine chemicals and specialty chemicals
- Production of new chemicals and materials
- Stereoselective synthesis, including enantioselective synthesis
- More diverse range of reaction specificity than for small-molecule catalysts
- Increased speed and selectivity of enzymatic reactions
- Creation of abiological reactions catalyzed by enzymes
A research team led by John Hartwig and Douglas Clark of Berkeley Lab has synthesized artificial metalloproteins containing non-biologic porphyrins. These modified metalloproteins can catalyze a wider range of biologic and abiologic reactions, with a variable precious metal placed at the center dictating the selectivity and efficiency of these processes. Because this process does not alter the protein conformation or the enzyme active site, these molecules are capable of catalyzing processes efficiently and with extreme specificity. Preparation of these molecules is both cost effective and well understood, making these artificial metalloproteins ideal for use in both research and production based sectors.
Proteins that contain a metal-porphyrin cofactor are deconstructed and the naturally occurring metal within the active site is replaced with an abiologic noble metal. The native structure of the protein is not altered, and reactants enter the fully functional active site. The artificial metalloenzyme within the protein would be able to perform a wider range functions, including transport, sensing, and catalysis. One such novel reaction this modified metalloprotein is able to catalyze is the insertion of a carbene into a carbon-hydrogen bond.
FOR MORE INFORMATION:
Yang, S. “On the path toward bionic enzymes,” Berkeley Lab NewsCenter, June 15, 2016.
DEVELOPMENT STAGE: Functional artificial metalloproteins have been created containing abiologic metals including Ru, Rh, and Ir through several rounds of directed evolution.
STATUS: Patent pending. Available for licensing or collaborative research.