Resonant response to temperature modulation for enzymatic dynamics characterization.
We consider enzymes involved in a three-state Michaelis-Menten kinetics and submitted to well-chosen temperature modulations of small amplitude. From the first-order amplitudes of concentration oscillations, we design a response function that is maximum for targeted values of the chemical relaxation times. This resonant function can be used to screen a large set of enzymes and identify the one governed by the desired kinetics. The method gives access to all the dynamical parameters of the targeted enzyme without resorting to a fit. We show how to estimate the precision of this parameter determination and give some hints for experimental validation.
Berthoumieux
H
H
Ecole Normale Supérieure, Département de Chimie, UMR 8640 CNRS ENS UPMC-Paris 6 PASTEUR, 24, rue Lhomond, 75231 Paris Cedex 05, France.
Antoine
C
C
Jullien
L
L
Lemarchand
A
A
D003198:Computer Simulation; D004789:Enzyme Activation; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D013696:Temperature
D004798:Enzymes