Manipulating single enzymes by an external harmonic force.
We study a Michaelis-Menten reaction for a single two-state enzyme molecule, whose transition rates between the two conformations are modulated by an harmonically oscillating external force. In particular, we obtain a range of optimal driving frequencies for changing the conformation of the enzyme, thereby controlling the enzymatic activity (i.e., product formation). This analysis demonstrates that it is, in principle, possible to obtain information about particular rates within the kinetic scheme.
Lomholt
Michael A
MA
Physics Department, University of Ottawa, 150 Louis Pasteur, Ottawa, ON, K1N 6N5, Canada.
Urbakh
Michael
M
Metzler
Ralf
R
Klafter
Joseph
J
D003198:Computer Simulation; D004789:Enzyme Activation; D004798:Enzymes / Q000737:chemistry* / Q000648:ultrastructure*; D007700:Kinetics; D008846:Micromanipulation / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D009991:Oscillometry / Q000379:methods; D010812:Physical Stimulation / Q000379:methods; D013314:Stress, Mechanical
D004798:Enzymes