Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B sub(12)-Dependent Ethanolamine Ammonia Lyase

The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B sub(12)-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture).