Conformational dynamics in enzymatic reactions
Department of Applied Physics, Chalmers University of
Technology S-412 96 Göteborg, Sweden
2 Boreskov Institute of Catalysis, Russian Academy of Sciences Novosibirsk 630090, Russia
Accepted: 31 October 2001
We present lattice Monte Carlo simulations of the product-formation step in a rapid enzymatic reaction occurring via the conventional Henri-Michaelis-Menten mechanism. The reaction is considered to be limited by reconfiguration of the enzyme structure. The effect of the conformational dynamics on the apparent parameters characterizing the reaction kinetics is demonstrated to be hidden. In particular, the pre-exponential factor of the reaction rate constant is nearly equal to that for elementary moves of the protein chain forming the enzyme.
PACS: 87.15.-v – Biomolecules: structure and physical properties / 05.40.-a – Fluctuation phenomena, random processes, noise, and Brownian motion / 05.50.+q – Lattice theory and statistics (Ising, Potts, etc.)
© EDP Sciences, 2002