Coupled motions in enzyme catalysis.
Recently, the hypothesis that protein motions are involved in enzymatic turnover has gained significant attention. We review cases where there is evidence that protein motions are rate-limiting in the overall catalytic cycle and examine experimental and theoretical evidence for how such motions enhance the probability of sampling the transition state configurations relative to the ground state. The impact of tunneling, the possible role of vibrational coupling and the value of conformational chemical landscapes are also scrutinized.
Nashine
Vishal C
VC
Department of Chemistry, The Pennsylvania State University, 414 Wartik Laboratory, University Park, PA 16802, USA.
Hammes-Schiffer
Sharon
S
Benkovic
Stephen J
SJ
D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D009068:Movement
D004798:Enzymes