Optics Research Group, Department of Imaging Science and Technology, Faculty of Applied Sciences, Delft University of Technology, Lorentzweg 1, 2628 CJ, Delft, The Netherlands.
Interdiscip Sci. 2011 Jun;3(2):79-90. doi: 10.1007/s12539-011-0063-z. Epub 2011 May 4.
This paper presents theoretical and simulation studies on controlling enzymatic reactions with photoswitchable inhibitors. It is found that the maximum attainable switching ratio (ratio of the steady state rates of product formation in the "on" and the "off" state) of a photoswitchable inhibitor is dependent on its photoswitching factor (ratio of the equilibrium constants of the photostationary states under the "off" and the "on" illuminations). Attachment of multiple photoswitchable groups to an inhibitor molecule increases the theoretically attainable switching ratio. The affinity of the enzyme for the substrate and the inhibitor is the rate-limiting factor of the switching between active and inactive states. Use of inhibitors with high enzyme affinity and photoswitchable groups with high photoswitching factor would provide high switching ratio. These results may help to design better systems for optical control of biochemical processes.
本文提出了用光开关抑制剂控制酶反应的理论和模拟研究。研究发现，光开关抑制剂的最大可达到的开关比（“开”和“关”状态下产物形成的稳态速率之比）取决于其光开关因子（“关”和“开”光照下光稳定态平衡常数之比）。将多个光开关基团连接到抑制剂分子上会增加理论上可达到的开关比。酶对底物和抑制剂的亲和力是在活性和非活性状态之间切换的限速因素。使用与酶具有高亲和力的抑制剂和光开关基团具有高光开关因子的抑制剂将提供高开关比。这些结果可能有助于设计更好的用于光控生化过程的系统。
