Lomholt Michael A, Urbakh Michael, Metzler Ralf, Klafter Joseph
Physics Department, University of Ottawa, 150 Louis Pasteur, Ottawa, ON, K1N 6N5, Canada.
Phys Rev Lett. 2007 Apr 20;98(16):168302. doi: 10.1103/PhysRevLett.98.168302. Epub 2007 Apr 19.
We study a Michaelis-Menten reaction for a single two-state enzyme molecule, whose transition rates between the two conformations are modulated by an harmonically oscillating external force. In particular, we obtain a range of optimal driving frequencies for changing the conformation of the enzyme, thereby controlling the enzymatic activity (i.e., product formation). This analysis demonstrates that it is, in principle, possible to obtain information about particular rates within the kinetic scheme.
我们研究了单个双态酶分子的米氏反应，该酶分子两种构象之间的转变速率受到简谐振荡外力的调制。特别地，我们获得了一系列用于改变酶构象的最佳驱动频率，从而控制酶活性（即产物形成）。该分析表明，原则上有可能获得动力学方案中特定速率的信息。
