RESEARCH

The research of the Stull lab primarily investigates the chemical mechanisms of enzymes that use riboflavin-derived cofactors. These so-called "flavoenzymes" each come with a built in reporter - the flavin prosthetic group above - that provides a real time spectrophotometric readout of the chemistry occurring in the active site of the enzyme. 

Our current interest is on the flavoenzyme nicotine oxidoreductase, which initiates a metabolic pathway that enables certain bacteria to grow on nicotine as a sole carbon and nitrogen source. Curiously, nicotine oxidoreductase is poorly re-oxidized by O2, unlike all of its oxidase homologs. Our goal is to understand the mechanistic basis for this poor reactivity with O2 as it has hindered the development of nicotine oxidoreductase-based tobacco cessation therapies.