Theory and simulation of diffusion-controlled Michaelis-Menten kinetics for a static enzyme in solution.
We develop a uniform theory for the many-particle diffusion-control effects on the Michaelis-Menten scheme in solution, based on the Gopich-Szabo relaxation-time approximation (Gopich, I. V.; Szabo, A. J. Chem. Phys. 2002, 117, 507). We extend the many-particle simulation algorithm to the Michaelis-Menten case by utilizing the Green function previously derived for excited-state reversible geminate recombination with different lifetimes (Gopich, I. V.; Agmon, N. J. Chem. Phys. 2000, 110, 10433). Running the simulation for representative parameter sets in the time domain and under steady-state conditions, we find poor agreement with classical kinetics but excellent agreement with some of the modern theories for bimolecular diffusion-influenced reactions. Our simulation algorithm can be readily extended to the biologically interesting case of dense patches of membrane-bound enzymes.
Park
Soohyung
S
Institute of Chemistry and the Fritz Haber Research Center, The Hebrew University, Jerusalem 91904, Israel.
Agmon
Noam
N
D003198:Computer Simulation; D004058:Diffusion; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D012996:Solutions; D013379:Substrate Specificity
D004798:Enzymes; D012996:Solutions