Single-molecule enzymology: stochastic Michaelis-Menten kinetics
Single-molecule enzymology: stochastic Michaelis-Menten kinetics
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DOI：
10.1016/s0301-4622(02)00145-x
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发表时间：
2002-12-10
影响因子：
3.8
通讯作者：
Elson, EL
中科院分区：
文献类型：
--
作者：
Qian, H;Elson, EL
我们提供了一个随机分析的单分子酶反应，遵循米氏动力学。我们发现，该系统可以表现出振荡行为的非平衡稳态在适当的底物浓度。随机模型包括酶动力学和底物周转动力学。讨论了底物存活概率与酶构象轨迹时间相关性之间的关系。确定性动力学在大底物浓度作为一个限制的随机模型。我们认为，除了波动的酶构象，底物浓度波动的随机性是另一个可能的来源，单分子酶动力学的复杂行为。(C)2002 Elsevier Science B.V.保留所有权利。
We provide a stochastic analysis of single-molecule enzymatic reactions that follow Michaelis-Menten kinetics. We show that this system can exhibit oscillatory behavior in the non-equilibrium steady-state at appropriate substrate concentrations. The stochastic model includes both enzyme dynamics and substrate turnover kinetics. The relationship between the probability of substrate survival and the time-correlation of enzyme conformation trajectories is discussed. Deterministic kinetics at large substrate concentrations are obtained as a limit of the stochastic model. We suggest that in addition to fluctuating enzyme conformation, the stochastic nature of substrate concentration fluctuations is another possible source of the complex behavior of single-molecule enzyme kinetics. (C) 2002 Elsevier Science B.V. All rights reserved.