N'-(3-biotinamidophenylsulfonyl)-ethylenediamine

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 生物素及其衍生物
• 英文名称: N'-(3-biotinamidophenylsulfonyl)-ethylenediamine
• 英文别名: 5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-N-[3-(2-aminoethylsulfamoyl)phenyl]pentanamide
• 化学式: C₁₈H₂₇N₅O₄S₂
• 分子量: 441.575
• InChiKey: YJTISOPXMFIAFT-ZOBUZTSGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  29
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  176
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  3-硝基苯磺酰氯 在 palladium on activated charcoal N-甲基吗啉 、 2-氯-4,6-二甲氧基-1,3,5-三嗪 、 氢气 、 三乙胺 、 三氟乙酸 作用下， 以 甲醇 、 二氯甲烷 、 乙腈 为溶剂， 20.0 ℃ 、300.0 kPa 条件下， 反应 36.0h， 生成 N'-(3-biotinamidophenylsulfonyl)-ethylenediamine
  参考文献：
  名称：

  Artificial Transfer Hydrogenases Based on the Biotin−(Strept)avidin Technology:  Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein

  摘要：

  Incorporation of biotinylated racemic three-legged d(6)-piano stool complexes in streptavidin yields enantioselective transfer hydrogenation artificial metalloenzymes for the reduction of ketones. Having identified the most promising organometallic catalyst precursors in the presence of wild-type streptavidin, fine-tuning of the selectivity is achieved by saturation mutagenesis at position S112. This choice for the genetic optimization site is suggested by docking studies which reveal that this position lies closest to the biotinylated metal upon incorporation into streptavidin. For aromatic ketones, the reaction proceeds smoothly to afford the corresponding enantioenriched alcohols in up to 97% ee (R) or 70% (S). On the basis of these results, we suggest that the enantioselection is mostly dictated by CH/pi interactions between the substrate and the eta(6)-bound arene. However, these enantiodiscriminating interactions can be outweighed in the presence of cationic residues at position S112 to afford the opposite enantiomers of the product.

  DOI：

  10.1021/ja061580o

文献信息

• Artificial Transfer Hydrogenases Based on the Biotin−(Strept)avidin Technology:  Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein
  作者：Christophe Letondor、Anca Pordea、Nicolas Humbert、Anita Ivanova、Sylwester Mazurek、Marjana Novic、Thomas R. Ward

  DOI：10.1021/ja061580o

  日期：2006.6.1

  Incorporation of biotinylated racemic three-legged d(6)-piano stool complexes in streptavidin yields enantioselective transfer hydrogenation artificial metalloenzymes for the reduction of ketones. Having identified the most promising organometallic catalyst precursors in the presence of wild-type streptavidin, fine-tuning of the selectivity is achieved by saturation mutagenesis at position S112. This choice for the genetic optimization site is suggested by docking studies which reveal that this position lies closest to the biotinylated metal upon incorporation into streptavidin. For aromatic ketones, the reaction proceeds smoothly to afford the corresponding enantioenriched alcohols in up to 97% ee (R) or 70% (S). On the basis of these results, we suggest that the enantioselection is mostly dictated by CH/pi interactions between the substrate and the eta(6)-bound arene. However, these enantiodiscriminating interactions can be outweighed in the presence of cationic residues at position S112 to afford the opposite enantiomers of the product.