tert-butyldimethylsilyloxy(N-phenylpyrrol-2-yl)acetonitrile

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯
• 英文名称: tert-butyldimethylsilyloxy(N-phenylpyrrol-2-yl)acetonitrile
• 英文别名: 2-[Tert-butyl(dimethyl)silyl]oxy-2-(1-phenylpyrrol-2-yl)acetonitrile；2-[tert-butyl(dimethyl)silyl]oxy-2-(1-phenylpyrrol-2-yl)acetonitrile
• 化学式: C₁₈H₂₄N₂OSi
• 分子量: 312.487
• InChiKey: AAFBJHLVEFHLEX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.06
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  38
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  1-苯-1H-吡咯-2-甲醛 在 咪唑 、 Amberlyst-A₂₁ 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 tert-butyldimethylsilyloxy(N-phenylpyrrol-2-yl)acetonitrile
  参考文献：
  名称：

  Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes

  摘要：

  The asymmetric hydrocyanation of pyrrole-2- and -3-carboxaldehydes substituted with either methyl, benzyl or phenyl in the I-position catalyzed by the hydroxynitrile lyases from Hevea brasiliensis (HbHNL) and Prunus amygdalus (PaHNL) is reported. The products could be isolated-after O-sitylation-with moderate to good enantiomeric purity although the carbon, I activity of the substrates was found to be very low, which is supported by quantum-chemical calculations. Structural effects concerning substrate size and regiochemistry are discussed considering docking calculations based on the X-ray crystal structures of the two enzymes. From these calculations one particular amino acid residue (Trp-128) in the active site of HbHNL could be identified, which plays a major role for the appropriate binding of structurally demanding carbonyl compounds. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2005.05.095

文献信息

• Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes
  作者：Thomas Purkarthofer、Karl Gruber、Martin H. Fechter、Herfried Griengl

  DOI：10.1016/j.tet.2005.05.095

  日期：2005.8

  The asymmetric hydrocyanation of pyrrole-2- and -3-carboxaldehydes substituted with either methyl, benzyl or phenyl in the I-position catalyzed by the hydroxynitrile lyases from Hevea brasiliensis (HbHNL) and Prunus amygdalus (PaHNL) is reported. The products could be isolated-after O-sitylation-with moderate to good enantiomeric purity although the carbon, I activity of the substrates was found to be very low, which is supported by quantum-chemical calculations. Structural effects concerning substrate size and regiochemistry are discussed considering docking calculations based on the X-ray crystal structures of the two enzymes. From these calculations one particular amino acid residue (Trp-128) in the active site of HbHNL could be identified, which plays a major role for the appropriate binding of structurally demanding carbonyl compounds. (c) 2005 Elsevier Ltd. All rights reserved.