(RS)-O-acetyl-1-phenyl-2-(methylseleno) ethanol | 56268-17-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (RS)-O-acetyl-1-phenyl-2-(methylseleno) ethanol
• 英文别名: (2-methylselanyl-1-phenylethyl) acetate
• CAS: 56268-17-8
• 化学式: C₁₁H₁₄O₂Se
• 分子量: 257.191
• InChiKey: UKNPTKIVRXCAOV-UHFFFAOYSA-N

物化性质

• 沸点：
  323.9±35.0 °C(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.46
• 重原子数：
  14.0
• 可旋转键数：
  4.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  26.3
• 氢给体数：
  0.0
• 氢受体数：
  2.0

反应信息

• 作为产物：
  描述：

  (RS)-1-苯基-2-(甲基硒)-乙醇 、 乙酸酐 在 吡啶 作用下， 反应 4.0h， 以92%的产率得到(RS)-O-acetyl-1-phenyl-2-(methylseleno) ethanol
  参考文献：
  名称：

  Enzymatic resolution of (RS)-β-hydroxy selenides in organic media

  摘要：

  Kinetic resolutions of a number of beta-hydroxy selenides promoted by enzymes were performed using PPL (free Porcine pancreatic lipase), PSL (Amano PS-free Pseudomonas sp. lipase) and CALB (NOVOZYM 435(R)-immobilized Candida Antarctica lipase type B) with (RS)-1-phenylselanyl-propan-2-ol. CALB gave the best results and provided both (R)- and (S)-enantiomers in high enantiomeric purity. A comparative study of the effect of temperature, solvent, enzyme immobilization and the structure of the substrates on the resolution is presented. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.11.007

文献信息

• Oxyselenation: reaction of olefins with dimethyl selenoxide
  作者：Noritaka Miyoshi、Seijiro Furui、Shinji Murai、Noboru Sonoda

  DOI：10.1039/c3975000293a

  日期：——

  The reaction of olefins with Me2SeO in AcOH–CHCl3 gave 2-acetoxyalkyl methyl selenides in good yields.

  烯烃与Me 2 SeO在AcOH-CHCl 3中的反应以良好的收率得到了2-乙酰氧基烷基甲基硒化物。
• Enzymatic resolution of (RS)-β-hydroxy selenides in organic media
  作者：Carlos E. Costa、Giuliano C. Clososki、Henrique B. Barchesi、Sandra P. Zanotto、M. Graça Nascimento、João V. Comasseto

  DOI：10.1016/j.tetasy.2004.11.007

  日期：2004.12

  Kinetic resolutions of a number of beta-hydroxy selenides promoted by enzymes were performed using PPL (free Porcine pancreatic lipase), PSL (Amano PS-free Pseudomonas sp. lipase) and CALB (NOVOZYM 435(R)-immobilized Candida Antarctica lipase type B) with (RS)-1-phenylselanyl-propan-2-ol. CALB gave the best results and provided both (R)- and (S)-enantiomers in high enantiomeric purity. A comparative study of the effect of temperature, solvent, enzyme immobilization and the structure of the substrates on the resolution is presented. (C) 2004 Elsevier Ltd. All rights reserved.