Structurally complex natural products, such as the medicinally relevant antibiotics vancomycin and erthromycin, are biosynthesized by large, macromolecular enzyme assemblies. These assemblies frequently orchestrate difficult and interesting chemical transformations to construct diverse molecular scaffolds. Our research group will use the tools of synthetic organic chemistry, enzymology and structural biology to dissect the mechanism of these systems. A detailed understanding of the biosynthesis of natural products will be extended to the development of new synthetic methodology and to the engineering of biological systems to produce novel molecules with desired properties.

Representative Key Publications:

Widboom, P. F.*, Fielding, E. N.*, Liu , Y., Bruner, S. D. “Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis” Nature, 2007, 447, p. 342-345.

Christianson, C. V., Montavon, T. J., Van Lanen, S. G., Shen, B., Bruner, S. D. "The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway" Biochemistry, 2007, 46, p. 7205-7214.

Liu , Y., Bruner, S. D. “Rational manipulation of carrier domain geometry in nonribosomal peptide synthetases” ChemBioChem, 2007, 8, p. 617-621.