Single-enzyme kinetics of CALB-catalyzed hydrolysis
Single-enzyme kinetics of CALB-catalyzed hydrolysis
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DOI：
10.1002/anie.200460625
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发表时间：
2005-01-01
影响因子：
16.6
通讯作者：
de Schryver, FC
中科院分区：
文献类型：
--
作者：
Velonia, K;Flomenbom, O;de Schryver, FC
深入了解化学过程的动态行为通常来自系综测量。然而，关于单分子水平动力学的直接实验信息很少，直到最近才主要从分子动力学模拟中推导出来。单分子光谱学的最新进展为探索化学反应过程中单个分子的行为铺平了道路。到目前为止，已经证明可以真实的实时监测单生物分子过程的动态行为，并观察一些运动蛋白、[1-5]氧化酶、[6]辣根过氧化物酶[7]和核酸酶的酶促周转。[8]最近，已经检测到单一黄素还原酶[9]和T4溶菌酶在反应过程中的结构波动[10]。这几个例子清楚地表明了在单分子水平上研究酶促过程的巨大潜力。
Insight into the dynamic behavior of chemical processes is typically derived from ensemble measurements. Direct experimental information about the dynamics at the singlemolecular level, however, is sparse and has until recently been primarily deduced from molecular-dynamics simulations. Current advances in single-molecule spectroscopy have paved the way for exploring the behavior of individual molecules in the course of a chemical reaction. Thus far it has proven possible to monitor in real time the dynamic behavior of single-biomolecular processes and observe the enzymatic turnovers of a few motor proteins,[1–5] an oxidase,[6] horseradish peroxidase,[7] and a nuclease.[8] More recently, structural fluctuations of a single flavin reductase [9] and of T4 lysozyme during the course of a reaction [10] have been detected. These few examples clearly demonstrate the tremendous potential of studying an enzymatic process at the single-molecular level.