3,3-dimethyl-2,3-dihydroindole-5,6-quinone-1,7d2 | 374756-99-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 3,3-dimethyl-2,3-dihydroindole-5,6-quinone-1,7d2
• CAS: 374756-99-7
• 化学式: C₁₀H₁₁NO₂
• 分子量: 179.187
• InChiKey: NLOYCACFGSYXTP-CWOYJHTQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.58
• 重原子数：
  13.0
• 可旋转键数：
  0.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  46.17
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  N,N-dideuterio-benzylamine 、 3,3-dimethyl-2,3-dihydroindole-5,6-quinone-1,7d2 在 氧气 作用下， 以 氘代甲醇 、 氘代乙腈 为溶剂， 反应 10.0h， 生成
  参考文献：
  名称：

  Catalytic Turnover of Benzylamine by a Model for the Lysine Tyrosylquinone (LTQ) Cofactor of Lysyl Oxidase

  摘要：

  Lysyl oxidase differs from other copper an-tine oxidases in that its active quinone cofactor reflects cross-linking of a lysyl residue into the tyrosine-derived quinone nucleus found in the plasma and other copper amine oxidases. A model for the lysyl oxidase cofactor (LTQ), 3,3-dimethyl-2,3-dihydroindole-5,6-quinone (4), was synthesized and found to be stable to both hydrolysis and oxidation events that prevent simpler models from functioning as turnover catalysts. We show that 4 catalyzes the aerobic oxidative deamination of benzylamine, though turnover eventually ceases on account of oxidation of the dihydrobenzoxazole tautomer of the "product Schiff base" to form a benzoxazole, a reaction that may be physiologically relevant. The mechanism of the overall reaction profile was elucidated by a combination of optical and NMR spectroscopy and O-2 uptake studies.

  DOI：

  10.1021/ja011141j
• 作为产物：
  描述：

  3,3-dimethyl-2,3-dihydroindole-5,6-quinone 在 氘代甲醇 、 三乙胺 作用下， 反应 0.17h， 生成 3,3-dimethyl-2,3-dihydroindole-5,6-quinone-1,7d2
  参考文献：
  名称：

  Catalytic Turnover of Benzylamine by a Model for the Lysine Tyrosylquinone (LTQ) Cofactor of Lysyl Oxidase

  摘要：

  Lysyl oxidase differs from other copper an-tine oxidases in that its active quinone cofactor reflects cross-linking of a lysyl residue into the tyrosine-derived quinone nucleus found in the plasma and other copper amine oxidases. A model for the lysyl oxidase cofactor (LTQ), 3,3-dimethyl-2,3-dihydroindole-5,6-quinone (4), was synthesized and found to be stable to both hydrolysis and oxidation events that prevent simpler models from functioning as turnover catalysts. We show that 4 catalyzes the aerobic oxidative deamination of benzylamine, though turnover eventually ceases on account of oxidation of the dihydrobenzoxazole tautomer of the "product Schiff base" to form a benzoxazole, a reaction that may be physiologically relevant. The mechanism of the overall reaction profile was elucidated by a combination of optical and NMR spectroscopy and O-2 uptake studies.

  DOI：

  10.1021/ja011141j