title: Fast enzyme dynamics at the active site of formate dehydrogenase.
abstract: The role of femtosecond-picosecond structural dynamics of proteins in enzyme-catalyzed reactions is a hotly debated topic. We report infrared photon echo measurement of the formate dehydrogenase-NAD+-azide ternary complex. In contrast to earlier studies of protein dynamics, the data show complete spectral diffusion on the femtosecond-picosecond time scale with no static heterogeneity. This result indicates that this transition-state analogue complex completely samples the distribution of structures that determine the distribution of azide vibrational frequencies within a few picoseconds and that there are no slower motions that perturb the H-bond network at the active site.
authors: Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242, USA.
authors: Jigar N
authors: JN
authors: Bandaria
authors: Samrat
authors: S
authors: Dutta
authors: Sarah E
authors: SE
authors: Hill
authors: Amnon
authors: A
authors: Kohen
authors: Christopher M
authors: CM
authors: Cheatum
mesh_terms: D001386:Azides / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002175:Candida / Q000737:chemistry; D002384:Catalysis; D004058:Diffusion; D005560:Formate Dehydrogenases / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry; D006860:Hydrogen Bonding; D007700:Kinetics; D013055:Spectrophotometry, Infrared
chemical_list: D001386:Azides; D005656:Fungal Proteins; D005560:Formate Dehydrogenases