Frederick W. Stull

This paper identifies two oxygen-dependent nicotine and pseudooxynicotine metabolizing enzymes with higher catalytic efficiency than NicA2, suggesting their potential for therapeutic and biotechnological applications.

This study traces the evolutionary emergence of oxidase activity in nicotine-degrading flavoenzymes by identifying key amino acid changes and their structural impacts.

This study identifies Glu292 and Lys331 as critical residues in NctB's catalytic mechanism, showing that Glu292 optimizes Lys331's role in dioxygen activation despite lacking the conserved lysine found in other FAO enzymes.

The paper shows that G-quadruplexes can catalyze protein folding without ATP, reshaping the energy landscape and suggesting a broader capacity for protein folding in cells.

The paper rationally designs a flavoenzyme Pnao with improved aerobic nicotine catabolism, showing activity in rat serum and identifying key residues for enzyme specificity.