Mutual synchronization of molecular turnover cycles in allosteric enzymes

被引:28
作者
Stange, P
Mikhailov, AS
Hess, B
机构
[1] Max Planck Gesell, Fritz Haber Inst, Chem Phys Abt, D-14195 Berlin, Germany
[2] Max Planck Inst Med Forsch, D-69120 Heidelberg, Germany
来源
JOURNAL OF PHYSICAL CHEMISTRY B | 1998年 / 102卷 / 32期
关键词
D O I
10.1021/jp9813185
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 diffusive transport and mixing times of regulatory molecules in micrometer and submicrometer_ reaction volumes can be shorter than characteristic times of conformational transformations in single enzyme molecules. Under these conditions, mutual synchronization of individual molecular turnover cycles takes place when strong allosteric activation by the reaction products is present. Using simple automaton models to describe the cycles of single molecules, we analyze properties of the synchronization transition and the role of statistical fluctuations in the synchronization phenomena.
引用
收藏
页码:6273 / 6289
页数:17
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