4-((E)-2-Chlorocarbonyl-vinyl)-benzoyl chloride | 166903-94-2

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: 4-((E)-2-Chlorocarbonyl-vinyl)-benzoyl chloride
• 英文别名: 4-[(E)-3-chloro-3-oxoprop-1-enyl]benzoyl chloride
• CAS: 166903-94-2
• 化学式: C₁₀H₆Cl₂O₂
• 分子量: 229.062
• InChiKey: OXFNIZCTQBUHGF-ZZXKWVIFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  34.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  4-((E)-2-Chlorocarbonyl-vinyl)-benzoyl chloride 在 sodium iodide 作用下， 以 四氢呋喃 、 乙腈 为溶剂， 反应 14.0h， 生成 [hydroxy(methoxy)phosphoryl] 4-[(E)-3-[hydroxy(methoxy)phosphoryl]oxy-3-oxoprop-1-enyl]benzoate
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z
• 作为产物：
  描述：

  trans-p-carboxycinnamic acid 在 草酰氯 、 N,N-二甲基甲酰胺 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 以92%的产率得到4-((E)-2-Chlorocarbonyl-vinyl)-benzoyl chloride
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z