(R)-benzyl ethyl sulfoxide | 28295-59-2

• 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: (R)-benzyl ethyl sulfoxide
• 英文别名: [(R)-ethylsulfinyl]methylbenzene
• CAS: 28295-59-2
• 化学式: C₉H₁₂OS
• 分子量: 168.26
• InChiKey: KCXODFMHDFXFSV-LLVKDONJSA-N

物化性质

• 沸点：
  339.4±21.0 °C(Predicted)
• 密度：
  1.134±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  11
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  36.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  benzyl ethyl sulfoxide 在 Escherichia coli with methionine sulfoxide reductase A 、 7b-dodecyl-7bH-benzo[d][1,2]oxazireno[2,3-b]isothiazole 3,3-dioxide 作用下， 以 癸烷 为溶剂， 反应 24.0h， 以59%的产率得到(R)-benzyl ethyl sulfoxide
  参考文献：
  名称：

  手性亚砜的化学酶脱氨作用

  摘要：

  高对映选择性酶甲硫氨酸亚砜还原酶A与恶唑烷型氧化剂组合在两相装置中，用于手性亚砜的脱硫。值得注意的 是，在多种底物上均观察到了较高的ee值，从而为合成对映体纯的亚砜提供了一条实用的途径。

  DOI：

  10.1002/anie.201805858

文献信息

• Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign
  作者：Gonzalo de Gonzalo、Christian Smit、Jianfeng Jin、Adriaan J. Minnaard、Marco W. Fraaije

  DOI：10.1039/c1cc14039f

  日期：——

  By cofactor redesign, self-sufficient monooxygenases could be prepared. Tight binding of N-alkylated flavins to riboflavin-binding protein results in the creation of artificial flavoenzymes capable of H2O2-driven enantioselective sulfoxidations. By altering the flavin structure, opposite enantioselectivities could be achieved, in accordance with the binding mode predicted by in silicoflavin-protein docking of the unnatural flavin cofactors. The study shows that cofactor redesign is a viable approach to create artificial flavoenzymes with unprecedented activities.

  通过辅因子重设计，可以制备自给自足的单氧化酶。N-烷基化黄素与核黄素结合蛋白的紧密结合会产生能够驱动过氧化氢进行对映选择性亚磺氧化反应的人工黄酶。通过改变黄素结构，可以实现相反的对映选择性，这与通过计算机模拟的不天然黄素辅因子的结合模式预测一致。该研究表明，辅因子重设计是一种创造具有前所未有活性的人工黄酶的可行方法。
• Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase
  作者：Ana Rioz-Martínez、Malgorzata Kopacz、Gonzalo de Gonzalo、Daniel E. Torres Pazmiño、Vicente Gotor、Marco W. Fraaije

  DOI：10.1039/c0ob00988a

  日期：——

  A bacterial flavin-containing monooxygenase (FMO), fused to phosphite dehydrogenase, has been used to explore its biocatalytic potential. The bifunctional biocatalyst could be expressed in high amounts in Escherichia coli and was able to oxidize indole and indole derivatives into a variety of indigo compounds. The monooxygenase also performs the sulfoxidation of a wide range of prochiral sulfides, showing moderate to good enantioselectivities in forming chiral sulfoxides.

  一种含黄素的单氧化酶（FMO）与磷酸脱氢酶融合，被用于探索其生物催化潜力。这种双功能生物催化剂能够在大肠杆菌中高量表达，并能够将吲哚及其衍生物氧化成多种靛蓝化合物。该单氧化酶还对多种前手性硫化物进行亚硫氧化，显示出中等到良好的选择性，能够形成手性亚硫氧化物。
• 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides
  作者：Gonzalo de Gonzalo、Daniel E. Torres Pazmiño、Gianluca Ottolina、Marco W. Fraaije、Giacomo Carrea

  DOI：10.1016/j.tetasy.2005.11.024

  日期：2006.1

  sulfoxidation reactions on a set of aromatic sulfides. With a few exceptions, excellent enantioselectivities in the synthesis of chiral phenyl and benzyl sulfoxides were achieved. The bacterial Baeyer–Villiger monooxygenase was also shown to accept racemic sulfoxides, a prochiral diketone and an organoboron compound as substrates. This study demonstrates the great biocatalytic potential of this novel oxidative

  来自荧光假单胞菌ACB的重组4-羟基苯乙酮单加氧酶（HAPMO）已作为一组芳族硫化物的硫氧化反应的催化剂进行了测试。除少数例外，在手性苯基和苄基亚砜的合成中获得了极好的对映选择性。细菌Baeyer-Villiger单加氧酶也被证明可以接受外消旋亚砜，前手性二酮和有机硼化合物作为底物。这项研究证明了这种新型氧化酶的巨大生物催化潜力。
• Expanding the toolbox of Baeyer–Villiger and flavin monooxygenase biocatalysts for the enantiodivergent green synthesis of sulfoxides
  作者：Jingyue Wu、Silvia Anselmi、Alexandra T. P. Carvalho、Jill Caswell、Derek J. Quinn、Thomas S. Moody、Daniele Castagnolo

  DOI：10.1039/d4gc02657h

  日期：——

  Two new monooxygenase biocatalysts, the Baeyer–Villiger monooxygenase BVMO145 and the flavin monooxygenase FMO401 from Almac library, have been found to catalyse the enantiodivergent oxidation of sulfides bearing N-heterocyclic substituents into sulfoxides under mild and green conditions. The biocatalyst BVMO145 provides (S)-sulfoxides while the flavin monooxygenase FMO401 affords (R)-sulfoxides with

  两种新的单加氧酶生物催化剂，Baeyer-Villiger 单加氧酶 BVMO145 和来自 Almac 库的黄素单加氧酶 FMO401，被发现可以在温和和绿色条件下催化带有 N-杂环取代基的硫化物对映异构氧化成亚砜。生物催化剂 BVMO145 提供 ( S )-亚砜，而黄素单加氧酶 FMO401 提供 ( R )-亚砜，具有良好的转化率和高 ee。
• Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca
  作者：Gonzalo de Gonzalo、Daniel E. Torres Pazmiño、Gianluca Ottolina、Marco W. Fraaije、Giacomo Carrea

  DOI：10.1016/j.tetasy.2005.08.004

  日期：2005.9

  Several organic sulfides, ketones and other organic systems have been tested as substrates in oxidation reactions catalyzed by the recently discovered phenylacetone monooxygenase from Thermobifida fusca. The biocatalytic properties of this Baeyer-Villiger monooxygenase have been studied, revealing reactivity with a large range of sulfides and ketones. Oxidations of several sulfoxides, an amine and an organoboron compound were also observed. The enzyme is able to oxidize a number of sulfides with excellent enantioselectivity, demonstrating the catalytic potential of this novel biocatalyst. (C) 2005 Elsevier Ltd. All rights reserved.