Fast enzyme dynamics at the active site of formate dehydrogenase.
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.
Bandaria
Jigar N
JN
Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242, USA.
Dutta
Samrat
S
Hill
Sarah E
SE
Kohen
Amnon
A
Cheatum
Christopher M
CM
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
D001386:Azides; D005656:Fungal Proteins; D005560:Formate Dehydrogenases