6-chloro-8-fluoro-4-methylumbelliferone | 1070868-28-8

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: 6-chloro-8-fluoro-4-methylumbelliferone
• 英文别名: 6-Chloro-8-fluoro-7-hydroxy-4-methylchromen-2-one；6-chloro-8-fluoro-7-hydroxy-4-methylchromen-2-one
• CAS: 1070868-28-8
• 化学式: C₁₀H₆ClFO₃
• 分子量: 228.607
• InChiKey: OFLRVHNBYUORPQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  15
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  6-chloro-8-fluoro-4-methylumbelliferone phosphate 在 acid phosphotase from Solanum tubersum 、 邻硝基苯甲醛 作用下， 以 aq. acetate buffer 为溶剂， 生成 6-chloro-8-fluoro-4-methylumbelliferone
  参考文献：
  名称：

  通过纳秒级激光诱导的pH跳跃提高远程控制酶活性的时间分辨率

  摘要：

  光作为远程控制酶激活的触发器，可提供较高的时间和空间分辨率。以酸性磷酸酶和6-氯-8-氟-4-甲基伞形酮磷酸盐为底物的已知酶体系被用来研究通过光诱导的pH跃迁提高酶激活时间分辨率的不同策略。因此，单脉冲脉冲持续时间为6 ns的激光脉冲激发通过2-硝基苯甲醛的重排瞬时质子释放而使酶活化了4倍。现在，激活实验的时间分辨率仅受检测系统的限制，而不再受激发步骤的限制。此外，

  DOI：

  10.1002/cctc.201402442

文献信息

• Photoswitching of Enzyme Activity by Laser-Induced pH-Jump
  作者：Stefanie Kohse、Antje Neubauer、Alexandra Pazidis、Stefan Lochbrunner、Udo Kragl

  DOI：10.1021/ja400700x

  日期：2013.6.26

  Controlled initiation of biochemical events and in particular of protein activity is a powerful tool in biochemical research. Specifically, optical trigger signals are an attractive approach for remote control of enzyme activity. We present a method for generating optical control of enzyme activity applicable to a widespread range of enzymes. The approach is based on short laser pulses as optical "switches" introducing an instantaneous change of the pH-value for activation of protein function. The pH-jump is induced by proton release from 2-nitrobenzaldehyde. Reaction conditions were chosen to yield a pH-jump of almost 3 units on switching from inactive to active conditions for the enzyme. In this experimental setup, irradiation can be realized without any loss of enzyme activity. Following this change in pH-value, a controlled activation of hydrolytic activity of acid phosphatase is successfully demonstrated. This application provides a general method for photocontrol of enzymatic function for proteins having a significant pH-profile. The kinetic data for the substrate 6-chloro-8-fluoro-4-methylumbelliferone phosphate are determined.