(4-氰基苯基)硫酸氢盐 | 31377-14-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机硫酸及其衍生物
• 中文名称: (4-氰基苯基)硫酸氢盐
• 英文名称: Benzonitrile, 4-(sulfooxy)-
• 英文别名: (4-cyanophenyl) hydrogen sulfate
• CAS: 31377-14-7
• 化学式: C₇H₅NO₄S
• 分子量: 199.187
• InChiKey: LVKQILHPKBSXMO-UHFFFAOYSA-N

物化性质

• 密度：
  1.61±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  13
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  95.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (4-氰基苯基)硫酸氢盐 以 various solvent(s) 为溶剂， 生成 sodium 4-cyanophenolate
  参考文献：
  名称：

  Do Electrostatic Interactions with Positively Charged Active Site Groups Tighten the Transition State for Enzymatic Phosphoryl Transfer?

  摘要：

  The effect of electrostatic interactions on the transition-state character for enzymatic phosphoryl transfer has been a subject of much debate. In this work, we investigate the transition state for alkaline phosphatase (AP) using linear free-energy relationships (LIFERs). We determined k(cat)/K-M for a series of aryl sulfate ester monoanions to obtain the Bronsted coefficient, beta(lg)., and compared the value to that obtained previously for a series of aryl phosphorothioate ester dianion substrates. Despite the difference in substrate charge, the observed Bronsted coefficients for AP-catalyzed aryl sulfate and aryl phosphorothioate hydrolysis (-0.76 +/- 0.14 and -0.77 +/- 0.10, respectively) are strikingly similar, with steric effects being responsible for the uncertainties in these values. Aryl sulfates and aryl phosphates react via similar loose transition states in solution. These observations suggest an apparent equivalency of the transition states for phosphorothioate and sulfate hydrolysis reactions at the AP active site and, thus, negligible effects of active site electrostatic interactions on charge distribution in the transition state.

  DOI：

  10.1021/ja0480421

文献信息

• Do Electrostatic Interactions with Positively Charged Active Site Groups Tighten the Transition State for Enzymatic Phosphoryl Transfer?
  作者：Ivana Nikolic-Hughes、Douglas C. Rees、Daniel Herschlag

  DOI：10.1021/ja0480421

  日期：2004.9.1

  The effect of electrostatic interactions on the transition-state character for enzymatic phosphoryl transfer has been a subject of much debate. In this work, we investigate the transition state for alkaline phosphatase (AP) using linear free-energy relationships (LIFERs). We determined k(cat)/K-M for a series of aryl sulfate ester monoanions to obtain the Bronsted coefficient, beta(lg)., and compared the value to that obtained previously for a series of aryl phosphorothioate ester dianion substrates. Despite the difference in substrate charge, the observed Bronsted coefficients for AP-catalyzed aryl sulfate and aryl phosphorothioate hydrolysis (-0.76 +/- 0.14 and -0.77 +/- 0.10, respectively) are strikingly similar, with steric effects being responsible for the uncertainties in these values. Aryl sulfates and aryl phosphates react via similar loose transition states in solution. These observations suggest an apparent equivalency of the transition states for phosphorothioate and sulfate hydrolysis reactions at the AP active site and, thus, negligible effects of active site electrostatic interactions on charge distribution in the transition state.