For full understanding of the molecular mechanisms of enzymatic reactions, it is crucial to obtain the detailed structural information of the active sites of proteins. Reaction-induced Fourier transform infrared (FTIR) difference spectroscopy, which detects minute changes in the infrared absorption upon some reaction, is a powerful method to investigate the structures and reactions in the active sites of proteins at the atomic and molecular levels. In particular, light-induced FTIR difference spectroscopy that uses light as a trigger to initiate reactions has been extensively used in the studies of molecular mechanisms of photosensitive proteins. In this review article, the methods of measurement and analysis of light-induced FTIR difference spectra are described and applications to the studies of photosensitive proteins are introduced.
抄録全体を表示