| 331716-50-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• CAS: 331716-50-8
• 化学式: C₇₁H₇₁FeN₄O₄
• 分子量: 1100.22
• InChiKey: BXKCTRZHEREVMN-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：

  在 间氯过氧苯甲酸 作用下， 以 四氢呋喃 为溶剂， 生成
  参考文献：
  名称：

  “ Hangman”卟啉用于组装血红素水通道模型。

  摘要：

  DOI：

  10.1021/ja003245k
• 作为产物：
  描述：

  在 sodium hydroxide 作用下， 以 甲苯 为溶剂， 反应 12.0h， 以92%的产率得到
  参考文献：
  名称：

  Proton-Coupled O−O Activation on a Redox Platform Bearing a Hydrogen-Bonding Scaffold

  摘要：

  Porphyrin architectures bearing a hydrogen-bonding scaffold have been synthesized. The H-bond pendant allows proton-coupled electron transfer (PCET) to be utilized as a vehicle for effecting catalytic O-O bond activation chemistry. Suzuki cross-coupling reactions provide a modular synthetic strategy for the attachment of porphyrins to a rigid xanthene or dibenzofuran pillar bearing the H-bond pendant. The resulting HPX (hanging porphyrin xanthene) and HPD (hanging porphyrin dibenzofuran) systems permit both the orientation and acid-base properties of the hanging H-bonding group to be controlled. Comparative reactivity studies for the catalase-like disproportionation of hydrogen peroxide and the epoxidation of olefins by the HPX and HPD platforms with acid and ester hanging groups reveal that the introduction of a proton-transfer network, properly oriented to a redox-active platform, can orchestrate catalytic O-O bond activation. For the catalase and epoxidation reaction types, a marked reactivity enhancement is observed for the xanthene-bridged platform appended with a pendant carboxylic acid group, establishing that this approach can yield superior catalysts to analogues that do not control both proton and electron inventories.

  DOI：

  10.1021/ja028548o

文献信息

• Proton-Directed Redox Control of O−O Bond Activation by Heme Hydroperoxidase Models
  作者：Jake D. Soper、Sergey V. Kryatov、Elena V. Rybak-Akimova、Daniel G. Nocera

  DOI：10.1021/ja0683032

  日期：2007.4.1

  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.