[Fe(II)(bis(2-pyridylmethyl)glycinamide)(O2CCH3)(CH3OH)](BPh4) | 199106-22-4

• 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(II)(bis(2-pyridylmethyl)glycinamide)(O2CCH3)(CH3OH)](BPh4)
• CAS: 199106-22-4
• 化学式: C₁₇H₂₃FeN₄O₄*C₂₄H₂₀B
• 分子量: 722.475
• InChiKey: NZXPUDDBUSNYIQ-UHFFFAOYSA-M

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：

  [Fe(II)(bis(2-pyridylmethyl)glycinamide)(O2CCH3)(CH3OH)](BPh4) 、 氧气 以 not given 为溶剂， 生成 [Fe(III)2(μ-O)(.mu-O2CCH3)(bis(2-pyridylmethyl)glycinamide)2](ClO4)3
  参考文献：
  名称：

  Models for Amide Ligation in Nonheme Iron Enzymes

  摘要：

  Lipoxygenase and isopenicillin N synthase belong to an emerging class of mononuclear nonheme iron(II) enzymes involved in dioxygen activation.(1) Though these two enzymes catalyze very different reactions, they possess common structural features. Crystal structures(2,3) of these enzymes (Figure 1) show the divalent metal centers to be coordinated to a 2-His-1-carboxylate facial triad(1c) as well as an amide Ligand. These enzymes represent the first examples of amide ligation to iron in biology, a feature not anticipated by prior spectroscopic studies. The amide ligand appears to play a role in catalysis, as indicated by site-directed mutagenesis studies of the two (4,5) To determine the effects of an amide ligand an enzymes. the properties of an iron center, we have synthesized iron complexes of the tetradentate ligand bis(2-pyridylmethyl)glycinamide(BPh4). [Fe-II(BPGm)(0(2)CCH(3))(CH3OH)](BPh4) (1) represents the first example of a complex with a ligand combination that corresponds closely to the coordination environments found for the metal centers in lipoxygenase and isopenicillin N synthase. For comparison, we also report the structures of [Fe-II(TPA)(O2CC(CH3)(3))(CH3OH)](BPh4) (2, TPA = tris(2-pyridylmethyl)amine) and [Fe-2(III)(mu-O)(mu-O2CCH3)-(BPGm)(2)](ClO4)(3) (3) and their properties.

  DOI：

  10.1021/ic970541y
• 作为产物：
  描述：

  甲醇 、 ferrous perchlorate 、 bis(2-pyridylmethyl)glycinamide 、 sodium acetate 、 四苯硼钠 以 甲醇 为溶剂， 生成 [Fe(II)(bis(2-pyridylmethyl)glycinamide)(O2CCH3)(CH3OH)](BPh4)
  参考文献：
  名称：

  Models for Amide Ligation in Nonheme Iron Enzymes

  摘要：

  Lipoxygenase and isopenicillin N synthase belong to an emerging class of mononuclear nonheme iron(II) enzymes involved in dioxygen activation.(1) Though these two enzymes catalyze very different reactions, they possess common structural features. Crystal structures(2,3) of these enzymes (Figure 1) show the divalent metal centers to be coordinated to a 2-His-1-carboxylate facial triad(1c) as well as an amide Ligand. These enzymes represent the first examples of amide ligation to iron in biology, a feature not anticipated by prior spectroscopic studies. The amide ligand appears to play a role in catalysis, as indicated by site-directed mutagenesis studies of the two (4,5) To determine the effects of an amide ligand an enzymes. the properties of an iron center, we have synthesized iron complexes of the tetradentate ligand bis(2-pyridylmethyl)glycinamide(BPh4). [Fe-II(BPGm)(0(2)CCH(3))(CH3OH)](BPh4) (1) represents the first example of a complex with a ligand combination that corresponds closely to the coordination environments found for the metal centers in lipoxygenase and isopenicillin N synthase. For comparison, we also report the structures of [Fe-II(TPA)(O2CC(CH3)(3))(CH3OH)](BPh4) (2, TPA = tris(2-pyridylmethyl)amine) and [Fe-2(III)(mu-O)(mu-O2CCH3)-(BPGm)(2)](ClO4)(3) (3) and their properties.

  DOI：

  10.1021/ic970541y