Biosynthetic Inorganic Chemistry
Potential Tuning
Heteronuclear Metalloenzymes
Unnatural Amino Acids and Non-Native Cofactors
The biosynthetic approach to inorganic chemistry makes use of proteins as ligands for catalytic metal centers. We believe that there are many advantages the biosynthetic approach in terms of physiological relevance, robustness, and the ability to tune long-rage effects beyond the first metal coordination shell. In the Lu protein lab, we focus on designing environmentally benign catalysts with applications in renewable energy generation and small molecule activation or transformation. For example, we are interested in designing metalloproteins with tunable redox potentials and their applications in many chemical and biological processes from efficient electron transfer (ET) agents in photosynthesis and respiration to catalysis in water oxidation and N2 fixation. In addition, we have designed biosynthetic models of heteronuclear metalloenzymes such as heme-copper oxidases (HCO) that are efficient biofuel cells, nitric oxide reductases (NOR) involved in the nitrogen cycle, and manganese peroxidases involved in biomass conversion. Finally, we are introducing unnatural amino acids and non-native cofactors, including many inorganic and organometallic catalysts, to make them water-soluble, asymmetric catalysts for applications such as synthesizing chiral intermediates in pharmaceutical drugs.

For in-depth reviews of our research, please see our recent publications in
Curr. Opin. Chem. Biol, BBA-Bioenergetics, Nature, Inorganic Chemistry, and Angewandte Chemie

A presentation by Dr. Lu about the details of our process may also be viewed below.
(Click Title to View the Presentation)