ethyl 2-(3-trifluoroacetylphenyl)hydrazinecarboxylate | 236386-25-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: ethyl 2-(3-trifluoroacetylphenyl)hydrazinecarboxylate
• 英文别名: ethyl N-[3-(2,2,2-trifluoroacetyl)anilino]carbamate
• CAS: 236386-25-7
• 化学式: C₁₁H₁₁F₃N₂O₃
• 分子量: 276.215
• InChiKey: QFDGVKRMPBQKBM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  19.0
• 可旋转键数：
  4.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  67.43
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  ethyl 2-(3-trifluoroacetylphenyl)hydrazinecarboxylate 在 吡啶 、 盐酸羟胺 作用下， 以 乙醇 为溶剂， 反应 2.0h， 以98%的产率得到ethyl 2-(3-trifluoroacetyloximephenyl)hydrazinecarboxylate
  参考文献：
  名称：

  Trifluoromethyldiazirinylphenyldiazenes:  New Hemoprotein Active-Site Probes

  摘要：

  The photoactivatable trifluoromethyldiazirinylphenyldiazene probes 1a and 2a have been synthesized, and their utility in the mapping of hemoprotein active sites has been validated with myoglobin (Mb). Reaction of the probes with Mb yields Fe-aryl adducts. Photolysis of these adducts unmasks a carbene that cross-links to active-site protein residues. Migration of the aryl group from the iron to a porphyrin nitrogen then attaches the porphyrin chromophore to the labeled amino acid residue. Tryptic digestion of the labeled proteins followed by mass spectrometric analysis of the peptides has identified Leu-29, His-64, Ile-107, and Val-68 as active-site residues. Previous studies with an arylnitrene probe, which appears to only react with nucleophilic groups, identified His-64 as an active-site residue [Tschirret-Guth, R. A.; Medzihradszky, K. F.; Ortiz de Montellano, P. R. J. Am. Chem. Sec. 1998, 120, 7404-7410]. These studies have identified all but one of the active-site amino acids in contact with the probe. The present strategy not only labels active-site amino acids but also, because the probe is rigidly held in the active site, provides approximate locations for the labeled residues with respect to the heme iron atom. Validation of the Strategy with myoglobin opens the way to use of the approach with hemoproteins of unknown active-site structure.

  DOI：

  10.1021/ja990351h
• 作为产物：
  描述：

  1-(3-aminophenyl)-2,2,2-trifluoroethanone 在 吡啶 、 盐酸 、 tin(ll) chloride 、 sodium nitrite 作用下， 以 乙腈 为溶剂， 反应 0.57h， 生成 ethyl 2-(3-trifluoroacetylphenyl)hydrazinecarboxylate
  参考文献：
  名称：

  Trifluoromethyldiazirinylphenyldiazenes:  New Hemoprotein Active-Site Probes

  摘要：

  The photoactivatable trifluoromethyldiazirinylphenyldiazene probes 1a and 2a have been synthesized, and their utility in the mapping of hemoprotein active sites has been validated with myoglobin (Mb). Reaction of the probes with Mb yields Fe-aryl adducts. Photolysis of these adducts unmasks a carbene that cross-links to active-site protein residues. Migration of the aryl group from the iron to a porphyrin nitrogen then attaches the porphyrin chromophore to the labeled amino acid residue. Tryptic digestion of the labeled proteins followed by mass spectrometric analysis of the peptides has identified Leu-29, His-64, Ile-107, and Val-68 as active-site residues. Previous studies with an arylnitrene probe, which appears to only react with nucleophilic groups, identified His-64 as an active-site residue [Tschirret-Guth, R. A.; Medzihradszky, K. F.; Ortiz de Montellano, P. R. J. Am. Chem. Sec. 1998, 120, 7404-7410]. These studies have identified all but one of the active-site amino acids in contact with the probe. The present strategy not only labels active-site amino acids but also, because the probe is rigidly held in the active site, provides approximate locations for the labeled residues with respect to the heme iron atom. Validation of the Strategy with myoglobin opens the way to use of the approach with hemoproteins of unknown active-site structure.

  DOI：

  10.1021/ja990351h