Contact Us
Department of Chemistry
101 N. Merion Ave
Bryn Mawr, PA 19010
610-526-7392, or
Fax: 610-526-5086

Yan Kung

In the Kung lab, our aim is to gain molecular insight into the function of enzymes by determining and examining their three-dimensional structures. By studying enzyme structures using X-ray crystallography while interrogating their functions with complementary biochemical techniques, we can develop a chemical understanding of enzyme catalysis. Enzyme systems of particular interest in the Kung lab include those that are involved in producing molecules that are useful to society, such as drug or biofuel compounds. Armed with a deep awareness of how an enzyme’s structure dictates its function, we may even engineer the enzyme in order to alter its function, allowing us to design modified enzymes that are tailor-made to produce more desirable drugs or biofuels.

Lab Website: Coming Soon!

Selected Publications

Kung, Y., Ando, N., Doukov, T.I., Blasiak, L.C., Seravalli, J., Bender, G., Ragsdale, S.W., and Drennan, C.L. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature. 48, 265-269. Link.

Kung, Y., Runguphan, W., and Keasling, J.D. (2012) From fields to fuels: Recent advances in the microbial production of biofuels. ACS Synth. Biol. 1, 498-513. Link.

Ando, N., Kung, Y., Can, M., Bender, G., Ragsdale, S.W., and Drennan, C.L. (2012) Transient B12-dependent methyltransferase complexes revealed by small-angle X-ray scattering. J. Am. Chem. Soc. 134, 17945-17954. Link.

Kung, Y. and Drennan, C.L. (2011) A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization. Curr. Opin. Chem. Biol. 15, 276-283. Link.

Kung, Y., Doukov, T.I., Seravalli, J., Ragsdale, S.W., and Drennan, C.L. (2009) Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 48, 7432-7440. Link.