Single-Enzyme Kinetics of CALB-Catalyzed Hydrolysis

摘要

Insight into the dynamic behavior of chemical processes is typically derived from ensemble measurements. Direct experimental information about the dynamics at the single-molecular level, however, is sparse and has until recently been primarily deduced from molecular-dynamics simulations. Current advances in single-molecule spectroscopy have paved the way for exploring the behavior of individual molecules in the course of a chemical reaction. Thus far it has proven possible to monitor in real time the dynamic behavior of single-biomolecular processes and observe the enzymatic turnovers of a few motor proteins,[1]-[5] an oxidase,[6] horseradish peroxidase,[7] and a nuclease.[8] More recently, structural fluctuations of a single flavin reductase[9] and of T4 lysozyme during the course of a reaction[10] have been detected. These few examples clearly demonstrate the tremendous potential of studying an enzymatic process at the single-molecular level.