| 938170-24-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• CAS: 938170-24-2
• 化学式: C₇₈H₇₄ClFeN₄O₆
• 分子量: 1254.77
• InChiKey: IGRSFBCFHWTAHY-CJGWQYIDSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
  None
• 可旋转键数：
  None
• 环数：
  None
• sp3杂化的碳原子比例：
  None
• 拓扑面积：
  None
• 氢给体数：
  None
• 氢受体数：
  None

反应信息

• 作为反应物：
  描述：

  以 二氯甲烷 为溶剂， 生成
  参考文献：
  名称：

  Proton-Directed Redox Control of O−O Bond Activation by Heme Hydroperoxidase Models

  摘要：

  Hangman metalloporphyrin complexes poise an acid-base group over a redox-active metal center and in doing so allow the "pull" effect of the secondary coordination environment of the heme cofactor of hydroperoxidase enzymes to be modeled. Stopped-flow investigations have been performed to decipher the influence of a proton-donor group on O-O bond activation. Low-temperature reactions of tetramesitylporphyrin (TMP) and Hangman iron complexes containing acid (HPX-CO2H) and methyl ester (HPX-CO2Me) functional groups with peroxyacids generate high-valent FeO active sites. Reactions of peroxyacids with (TMP)Fe-III(OH) and methyl ester Hangman (HPX-CO2Me)Fe-III(OH) give both O-O heterolysis and homolysis products, Compound I (Cpd I) and Compound II (Cpd II), respectively. However, only the former is observed when the hanging group is the acid, (HPX-CO2H)Fe-III(OH), because odd-electron homolytic O-O bond cleavage is inhibited. This proton-controlled, 2e(-) (heterolysis) vs 1e(-) (homolysis) redox specificity sheds light on the exceptional catalytic performance of the Hangman metalloporphyrin complexes and provides tangible benchmarks for using proton-coupled multielectron reactions to catalyze O-O bond-breaking and bond-making reactions.

  DOI：

  10.1021/ja0683032
• 作为产物：
  描述：

  、 间氯过氧苯甲酸 以 二氯甲烷 为溶剂， 生成
  参考文献：
  名称：

  Proton-Directed Redox Control of O−O Bond Activation by Heme Hydroperoxidase Models

  摘要：

  Hangman metalloporphyrin complexes poise an acid-base group over a redox-active metal center and in doing so allow the "pull" effect of the secondary coordination environment of the heme cofactor of hydroperoxidase enzymes to be modeled. Stopped-flow investigations have been performed to decipher the influence of a proton-donor group on O-O bond activation. Low-temperature reactions of tetramesitylporphyrin (TMP) and Hangman iron complexes containing acid (HPX-CO2H) and methyl ester (HPX-CO2Me) functional groups with peroxyacids generate high-valent FeO active sites. Reactions of peroxyacids with (TMP)Fe-III(OH) and methyl ester Hangman (HPX-CO2Me)Fe-III(OH) give both O-O heterolysis and homolysis products, Compound I (Cpd I) and Compound II (Cpd II), respectively. However, only the former is observed when the hanging group is the acid, (HPX-CO2H)Fe-III(OH), because odd-electron homolytic O-O bond cleavage is inhibited. This proton-controlled, 2e(-) (heterolysis) vs 1e(-) (homolysis) redox specificity sheds light on the exceptional catalytic performance of the Hangman metalloporphyrin complexes and provides tangible benchmarks for using proton-coupled multielectron reactions to catalyze O-O bond-breaking and bond-making reactions.

  DOI：

  10.1021/ja0683032