My research interests are in the area of mechanistic enzymology of redox enzymes with a specific interest in flavin-dependent enzymes. My objective is to understand how enzymes can influence the energetics of reaction intermediates and transition states. These aspects are being studied by steady state and pre-steady state kinetics using isotopically enriched substrates and substrate analogs.
Molecular oxygen acts as the final electron acceptor.
The enzyme has been found in bacteria of the genera Arthrobacter sp. Furthermore, the development of biosensors for the detection of choline and choline derivatives in serological samples renders this enzyme of medical and clinical interest. From a chemical standpoint, the mechanism of cleavage of the carbon-hydrogen bond of the substrate by choline oxidase is of particular interest because of the high energetic barrier associated with this process. Despite these reasons, choline oxidase is poorly characterized. The Arthrobacter choline oxidase has been cloned in E. coli by the group of Dr. Murata, National Institute for Basic Biology, Okazaki, Japan.