3-benzyl-5-bromo-6-methylpyrazin-2-amine | 902135-42-6

• 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-benzyl-5-bromo-6-methylpyrazin-2-amine
• 英文别名: 3-Benzyl-5-bromo-6-methylpyrazin-2-amine
• CAS: 902135-42-6
• 化学式: C₁₂H₁₂BrN₃
• 分子量: 278.151
• InChiKey: MHFFLEXYTJPAKW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  16
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  51.8
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  3-benzyl-5-bromo-6-methylpyrazin-2-amine 在 四(三苯基膦)钯 吡啶 、 sodium carbonate 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 为溶剂， 反应 3.5h， 生成 3-benzyl-5-(4-benzyloxy)phenyl-6-methyl-2-(octanamido)pyrazine
  参考文献：
  名称：

  Real light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin: light emission from the singlet-excited state of coelenteramide phenolate anion in a contact ion pair

  摘要：

  Fluorescence of the phenolate anion (3(O)(-)) and the amide anion (5(N)(-)) of coelenteramide analogues in ion pairs with various counter cations was systematically investigated to elucidate the ionic structure of the light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin. The fluorescent properties of 3(O)- in an ion pair with a conjugate acid of an organic base (BASE-H+) were varied depending on the structural variation of the ion pair and the solvent polarity. In particular, the fluorescence of 3(O)- in the ion pair with the conjugate acid of n-butylamine (NBA-H+) indicates that the singlet-excited state of 3(O)(-) ((1)3(O)(-)*) and NBA-H+ make a contact ion pair in which the fluorescence emission maxima of 3(O)- is sensitive to the solvent polarity and the fluorescence quantum yields of 3(O)- increase in a less polar solvent. The results also confirm that (1)3(O)-* is a twisted intramolecular charge transfer state. By contrast, the fluorescence of 5(N)(-) in an ion pair depends little on the BASE-H+ or the solvent polarity. Based on these results, we conclude that the light emitter in aequorin and obelin bioluminescences is the singlet-excited state of coelenteramide phenolate anion 2(O)(-)((1)2(O)(-)*) in a contact ion pair with an imidazolium side chain of a histidine residue, which is located at the less polar active sites of the photoproteins. We also propose a mechanism for the bioluminescence reaction, including the chemiexcitation process to give (1)2(O)(-)*. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2006.04.044
• 作为产物：
  描述：

  2-氨基-6-甲基吡嗪 在 bis-triphenylphosphine-palladium(II) chloride 吡啶 、 tetra-N-butylammonium tribromide 作用下， 以 氯仿 、 N,N-二甲基甲酰胺 为溶剂， 反应 5.5h， 生成 3-benzyl-5-bromo-6-methylpyrazin-2-amine
  参考文献：
  名称：

  Real light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin: light emission from the singlet-excited state of coelenteramide phenolate anion in a contact ion pair

  摘要：

  Fluorescence of the phenolate anion (3(O)(-)) and the amide anion (5(N)(-)) of coelenteramide analogues in ion pairs with various counter cations was systematically investigated to elucidate the ionic structure of the light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin. The fluorescent properties of 3(O)- in an ion pair with a conjugate acid of an organic base (BASE-H+) were varied depending on the structural variation of the ion pair and the solvent polarity. In particular, the fluorescence of 3(O)- in the ion pair with the conjugate acid of n-butylamine (NBA-H+) indicates that the singlet-excited state of 3(O)(-) ((1)3(O)(-)*) and NBA-H+ make a contact ion pair in which the fluorescence emission maxima of 3(O)- is sensitive to the solvent polarity and the fluorescence quantum yields of 3(O)- increase in a less polar solvent. The results also confirm that (1)3(O)-* is a twisted intramolecular charge transfer state. By contrast, the fluorescence of 5(N)(-) in an ion pair depends little on the BASE-H+ or the solvent polarity. Based on these results, we conclude that the light emitter in aequorin and obelin bioluminescences is the singlet-excited state of coelenteramide phenolate anion 2(O)(-)((1)2(O)(-)*) in a contact ion pair with an imidazolium side chain of a histidine residue, which is located at the less polar active sites of the photoproteins. We also propose a mechanism for the bioluminescence reaction, including the chemiexcitation process to give (1)2(O)(-)*. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2006.04.044

文献信息

• Real light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin: light emission from the singlet-excited state of coelenteramide phenolate anion in a contact ion pair
  作者：Kotaro Mori、Shojiro Maki、Haruki Niwa、Hiroshi Ikeda、Takashi Hirano

  DOI：10.1016/j.tet.2006.04.044

  日期：2006.6

  Fluorescence of the phenolate anion (3(O)(-)) and the amide anion (5(N)(-)) of coelenteramide analogues in ion pairs with various counter cations was systematically investigated to elucidate the ionic structure of the light emitter in the bioluminescence of the calcium-activated photoproteins aequorin and obelin. The fluorescent properties of 3(O)- in an ion pair with a conjugate acid of an organic base (BASE-H+) were varied depending on the structural variation of the ion pair and the solvent polarity. In particular, the fluorescence of 3(O)- in the ion pair with the conjugate acid of n-butylamine (NBA-H+) indicates that the singlet-excited state of 3(O)(-) ((1)3(O)(-)*) and NBA-H+ make a contact ion pair in which the fluorescence emission maxima of 3(O)- is sensitive to the solvent polarity and the fluorescence quantum yields of 3(O)- increase in a less polar solvent. The results also confirm that (1)3(O)-* is a twisted intramolecular charge transfer state. By contrast, the fluorescence of 5(N)(-) in an ion pair depends little on the BASE-H+ or the solvent polarity. Based on these results, we conclude that the light emitter in aequorin and obelin bioluminescences is the singlet-excited state of coelenteramide phenolate anion 2(O)(-)((1)2(O)(-)*) in a contact ion pair with an imidazolium side chain of a histidine residue, which is located at the less polar active sites of the photoproteins. We also propose a mechanism for the bioluminescence reaction, including the chemiexcitation process to give (1)2(O)(-)*. (c) 2006 Elsevier Ltd. All rights reserved.