1,4,6,7-四甲基-2,3-二氢喹喔啉 | 66102-32-7

• 分子结构分类: 有机化合物 - 有机氮化合物
• 中文名称: 1,4,6,7-四甲基-2,3-二氢喹喔啉
• 英文名称: 1,4,6,7-tetramethyl-1,2,3,4-tetrahydroquinoxaline
• 英文别名: Quinoxaline, 1,2,3,4-tetrahydro-1,4,6,7-tetramethyl-；1,4,6,7-tetramethyl-2,3-dihydroquinoxaline
• CAS: 66102-32-7
• 化学式: C₁₂H₁₈N₂
• 分子量: 190.288
• InChiKey: GRTNOUSOHQAZNZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  14
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  6.5
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  6,7-二甲基喹喔啉 、 聚合甲醛 在 sodium tetrahydroborate 、 三氟乙酸 作用下， 以 二氯甲烷 、 水 为溶剂， 反应 0.17h， 以31 mg的产率得到1,4,6,7-四甲基-2,3-二氢喹喔啉
  参考文献：
  名称：

  Long-Range Electron Transfer in Rigid 3₁₀-Helical Oligopeptides Containing Redox Cyclic a-Amino Acids

  摘要：

  AbstractIntrahelical photoinduced electron transfer processes (ET) in conformationally restricted oligopeptides have been studied by nanosecond time‐resolved transient spectroscopy. The helical peptides were constructed from ste‐rically hindered a‐aminoisobutyric acid (Aib) and two cyclic a‐amino acids (Aib class) bearing electron acceptor and donor side chains (DkNap, ThQx). This helical backbone design provides high conformation stability, as previously demonstrated, and yields reliable 310‐helical architectures in solution. The forward ET between ThQx and 3DkNap is followed by a slow back ET thus giving rise to an accumulation of the charge‐separated ion pairs for hundreds of nanoseconds. We demonstrate the modulation of electronic interactions by the number of intervening Aib residues separating acceptor‐donor side chains and propose modifications of the peptide framework by inclusion of a non‐Aib amino acid residue. These well‐defined and sterically stable frameworks are suited for the precise evaluation of intrahelical electron transfer processes mediated by peptides.

  DOI：

  10.1111/j.1751-1097.1999.tb08254.x

文献信息

• Long-Range Electron Transfer in Rigid 3₁₀-Helical Oligopeptides Containing Redox Cyclic a-Amino Acids
  作者：Kamil Lang、Atsuo Kuki

  DOI：10.1111/j.1751-1097.1999.tb08254.x

  日期：1999.10

  AbstractIntrahelical photoinduced electron transfer processes (ET) in conformationally restricted oligopeptides have been studied by nanosecond time‐resolved transient spectroscopy. The helical peptides were constructed from ste‐rically hindered a‐aminoisobutyric acid (Aib) and two cyclic a‐amino acids (Aib class) bearing electron acceptor and donor side chains (DkNap, ThQx). This helical backbone design provides high conformation stability, as previously demonstrated, and yields reliable 310‐helical architectures in solution. The forward ET between ThQx and 3DkNap is followed by a slow back ET thus giving rise to an accumulation of the charge‐separated ion pairs for hundreds of nanoseconds. We demonstrate the modulation of electronic interactions by the number of intervening Aib residues separating acceptor‐donor side chains and propose modifications of the peptide framework by inclusion of a non‐Aib amino acid residue. These well‐defined and sterically stable frameworks are suited for the precise evaluation of intrahelical electron transfer processes mediated by peptides.