A model of diffusion-influenced enzyme activation

被引:5
|
作者
Molski, A [1 ]
机构
[1] Adam Mickiewicz Univ, Dept Phys Chem, PL-60780 Poznan, Poland
来源
JOURNAL OF PHYSICAL CHEMISTRY B | 2000年 / 104卷 / 18期
关键词
D O I
10.1021/jp9935844
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The kinetics of a model of diffusion-influenced enzyme activation is studied in two spatial dimensions. Enzyme molecules diffuse and collide with an immobile, spherical, uniformly reactive receptor-ligand complex. Enzymes do not interact with each other, but interact with the complex via an interparticle potential. No hydrodynamic interactions are included. Inactive enzymes get activated upon collisions with the complex. Enzyme deactivation is modeled as a first-order kinetic process independent of diffusion and collisions, Exact expressions are derived for the steady-state number of active enzymes and for the Laplace transform of the time-dependent activation rate coefficient. The activation kinetics in the time domain can be calculated by numerical inversion of the kinetic expressions in Laplace space.
引用
收藏
页码:4532 / 4536
页数:5
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