A hypothesis concerning diffusion-limited protein-ligand interactions

被引:30
|
作者
van Holde, KE [1 ]
机构
[1] Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
关键词
kinetics; binding; oxygen; myoglobin; enzymes;
D O I
10.1016/S0301-4622(02)00176-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A simple assumption allows the prediction of the numerical value for a 'universal' limiting kinetic rate for wholly diffusion-limited reactions between small neutral molecules and macromolecules. This prediction is compared with appropriate experimental data for binding of ligands to myoglobin and to enzymes. It is shown that in the absence of electrostatic effects, this limit is approached but not exceeded. The model also makes very specific predictions concerning the viscosity and temperature dependence of such reactions. (C) 2002 Elsevier Science B.V. All rights reserved.
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页码:249 / 254
页数:6
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