Our group research interest lies in investigating basic mechanism of bio-active molecular (including nitric oxide, hydride and methyl et al.) transfer reaction in enzyme or in solution, with a goal of 1) design of more efficient chemical catalysis as well as the designed enzyme; 2) rational design of corresponding inhibitor/drug basing on the mechanism exploration.  This inspiring research area requires the combination the application of physical organic chemistry, biochemistry, chemical biology and molecular biology. 

   The most recently work refers to the understanding the role of compaction in methyl transfer reactions with the target of finding how the molecular motion in enzymes would affect the catalytic ability in the methyl transfer reaction.  This study about the methyl transfer system had/will extended from catechol-O-methyltransferase (COMT) to glycine-N-methyltransferase (GNMT), Nicotinamide N-Methyltransferase (NNMT) and DNA\RNA demethylation with various experimental approaches such kinetic isotope effect, binding isotope effect, time-resolved spectrometers, hydrogen deuterium exchange with mass spectrometry (HDX-MS) as well as computational simulation.