Chaudhury, Srabanti and Cherayil, Binny J (2007) Dynamic disorder in single-molecule Michaelis-Menten kinetics: The reaction-diffusion formalism in the Wilemski-Fixman approximation. In: Journal of Chemical Physics, 127 (10). pp. 105103-1.
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Single-molecule equations for the Michaelis-Menten [Biochem. Z. 49, 333 1913] mechanism of enzyme action are analyzed within the Wilemski-Fixman [J. Chem. Phys. 58, 4009 (1973); 60, 866 (1974) approximation after the effects of dynamic disorder—modeled by the anomalous diffusion of a particle in a harmonic well—are incorporated into the catalytic step of the reaction. The solution of the Michaelis-Menten equations is used to calculate the distribution of waiting times between successive catalytic turnovers in the enzyme \beta-galactosidase. The calculated distribution is found to agree qualitatively with experimental results on this enzyme obtained at four different substrate concentrations. The calculations are also consistent with measurements of correlations in the fluctuations of the fluorescent light emitted during the course of catalysis, and with measurements of the concentration dependence of the randomness parameter.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to American Institute of Physics.|
|Department/Centre:||Division of Chemical Sciences > Inorganic & Physical Chemistry|
|Date Deposited:||31 Jul 2008|
|Last Modified:||19 Sep 2010 04:48|
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