Fluctuating enzymes: lessons from single-molecule studies.
Recent single-molecule enzymology measurements with improved statistics have demonstrated that a single enzyme molecule exhibits large temporal fluctuations of the turnover rate constant at a broad range of time scales (from 1 ms to 100 s). The rate constant fluctuations, termed as dynamic disorder, are associated with fluctuations of the protein conformations observed on the same time scales. We discuss the unique information extractable from these experiments and the reconciliation of these observations with ensemble-averaged Michaelis-Menten equation. A theoretical model based on the generalized Langevin equation (GLE) treatment of Kramers' barrier crossing problem for chemical reactions accounts naturally for the observation of dynamic disorder and highly dispersed kinetics.
Min
Wei
W
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
English
Brian P
BP
Luo
Guobin
G
Cherayil
Binny J
BJ
Kou
S C
SC
Xie
X Sunney
XS
D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical
D004798:Enzymes