[Fe(N-propanoate-N,N-bis(2-pyridylmethyl)amine)]ClO4 | 1313513-85-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: [Fe(N-propanoate-N,N-bis(2-pyridylmethyl)amine)]ClO4
• CAS: 1313513-85-7
• 化学式: C₁₅H₁₆FeN₃O₂*ClO₄
• 分子量: 425.609
• InChiKey: JZWLRSMQKROLEJ-UHFFFAOYSA-L

计算性质

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

反应信息

• 作为反应物：
  描述：

  [Fe(N-propanoate-N,N-bis(2-pyridylmethyl)amine)]ClO4 、 氧化亚氮 以 not given 为溶剂， 生成 [Fe(N-propanoate-N,N-bis(2-pyridylmethyl)amine)(NO)]ClO4
  参考文献：
  名称：

  Structural and Electronic Characterization of Non-Heme Fe(II)–Nitrosyls as Biomimetic Models of the Fe_B Center of Bacterial Nitric Oxide Reductase

  摘要：

  The detoxification of nitric oxide (NO) by bacterial NO reductase (NorBC) has gained much attention as this reaction provides a paradigm as to how NO can be detoxified anaerobically in cells. However, a dear mechanistic picture of how the heme/non-heme active site of NorBC activates NO is lacking, mostly as a result of insufficient knowledge about the properties of the non-heme iron(II)-NO adduct. Here we report the first biomimetic model complexes for this species that closely resemble the coordination environment found in the protein, using the ligands BMPA-Pr and TPA. The systematic investigation of these compounds allowed us to gain key insight into the electronic structure and geometric properties of high-spin non-heme iron(II)-NO adducts. In particular, we show how small changes in the ligand environment of iron could be used by NorBC to greatly modulate the properties, and hence, the reactivity of this species.

  DOI：

  10.1021/ja111693f
• 作为产物：
  描述：

  ferrous perchlorate 、 N,N-bis(2-pyridylmethyl)3-aminopropionic acid 以 not given 为溶剂， 生成 [Fe(N-propanoate-N,N-bis(2-pyridylmethyl)amine)]ClO4
  参考文献：
  名称：

  Structural and Electronic Characterization of Non-Heme Fe(II)–Nitrosyls as Biomimetic Models of the Fe_B Center of Bacterial Nitric Oxide Reductase

  摘要：

  The detoxification of nitric oxide (NO) by bacterial NO reductase (NorBC) has gained much attention as this reaction provides a paradigm as to how NO can be detoxified anaerobically in cells. However, a dear mechanistic picture of how the heme/non-heme active site of NorBC activates NO is lacking, mostly as a result of insufficient knowledge about the properties of the non-heme iron(II)-NO adduct. Here we report the first biomimetic model complexes for this species that closely resemble the coordination environment found in the protein, using the ligands BMPA-Pr and TPA. The systematic investigation of these compounds allowed us to gain key insight into the electronic structure and geometric properties of high-spin non-heme iron(II)-NO adducts. In particular, we show how small changes in the ligand environment of iron could be used by NorBC to greatly modulate the properties, and hence, the reactivity of this species.

  DOI：

  10.1021/ja111693f