Difluoromethionine

Difluoromethionine (DFM) is a fluorinated methionine analogue primarily utilized as a biophysical probe in biochemical and medicinal chemistry research. It is investigated for its enzymatic processing by enzymes such as *Trichomonas vaginalis methionine γ-lyase (TvMGL)*, where its interaction can lead to the production of reactive intermediates and contribute to cellular toxicity. DFM serves as a valuable tool in 19F NMR studies to elucidate protein structure, dynamics, and protein-ligand interactions. It can be bioincorporated into recombinant proteins, including *Pseudomonas aeruginosa azurin* and *Pseudomonas aeruginosa alkaline protease*, allowing researchers to study the impact of methionine replacement on enzyme kinetics, thermal stability, and reduction potential, often with minimal structural perturbation. Additionally, DFM has been used to label proteins like the *leucine-isoleucine-valine binding protein (LIV)* to explore conformational changes.