Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase

D. Groff, M.C. Thielges, S. Celliti, P.G. Schultz, F.E. Romesberg, Angew. Chem., Int., Ed., (2009) 48:3478-3481.
pubpic2009groffSite-specific deuteration and FT-IR studies reveal that Tyr100 in DHFR plays an important role in catalysis, with a strong electrostatic coupling occuring between Tyr100 and the charge that develops in the hydride-transfer transition state.


Carbon-Deuterium bonds as probes of dihydrofolate reductase

M.C. Thielges, D.A. Case, F.E. Romesberg, J. Am. Chem. Soc. (2008) 130:6597-6603.
pubpic2008thielgesWe report a preliminary analysis of (methyl-d3) methionine residues, Met16, Met20, and Met42, within DHFR. The results confirm the sensitivity of the carbon−deuterium bonds to their local protein environment and demonstrate that dihydrofolate reductase is electrostatically and dynamically heterogeneous.