| 1427514-53-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯
• CAS: 1427514-53-1
• 化学式: C₂₈H₃₄F₃FeN₃O₄S
• 分子量: 621.504
• InChiKey: GMSUHFOWIPIMBI-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：
  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：

  、 氧化亚氮 以 四氢呋喃 为溶剂， 反应 0.5h， 以86%的产率得到
  参考文献：
  名称：

  The Functional Model Complex [Fe₂(BPMP)(OPr)(NO)₂](BPh₄)₂ Provides Insight into the Mechanism of Flavodiiron NO Reductases

  摘要：

  Flavodiiron nitric oxide reductases (FNORs), found in many pathogenic bacteria, are able to detoxify NO by reducing it to N2O. In this way, FNORs equip these pathogens with immunity to NO, which is a central immune defense agent in humans. Hence, FNORs are thought to promote infection of the human body, leading to chronic diseases. Despite this importance of FNORs for bacterial pathogenesis, the mechanism of NO reduction by these enzymes is not well understood. Here we present the synthesis and spectroscopic characterization of the diiron dinitrosyl model complex [Fe-2(BPMP)(OPr)(NO)(2)](BPh4)(2). The crystal structure of this complex shows two end-on-coordinated {FeNO}(7) units that, based on spectroscopic and electrochemical results, are only weakly electronically coupled. Importantly, reduction of this complex by two electrons leads to the clean formation of N2O in quantitative yield. This complex therefore represents the first example of a functional model system for FNORs. The results provide key mechanistic insight into the mechanism of FNORs and, in particular, represent strong support for the proposed "super-reduced" mechanism for these enzymes.

  DOI：

  10.1021/ja309782m
• 作为产物：
  描述：

  二甲基吡啶胺 在 sodium methylate 作用下， 以 甲醇 、 1,2-二氯乙烷 为溶剂， 反应 24.5h， 生成
  参考文献：
  名称：

  The Functional Model Complex [Fe₂(BPMP)(OPr)(NO)₂](BPh₄)₂ Provides Insight into the Mechanism of Flavodiiron NO Reductases

  摘要：

  Flavodiiron nitric oxide reductases (FNORs), found in many pathogenic bacteria, are able to detoxify NO by reducing it to N2O. In this way, FNORs equip these pathogens with immunity to NO, which is a central immune defense agent in humans. Hence, FNORs are thought to promote infection of the human body, leading to chronic diseases. Despite this importance of FNORs for bacterial pathogenesis, the mechanism of NO reduction by these enzymes is not well understood. Here we present the synthesis and spectroscopic characterization of the diiron dinitrosyl model complex [Fe-2(BPMP)(OPr)(NO)(2)](BPh4)(2). The crystal structure of this complex shows two end-on-coordinated {FeNO}(7) units that, based on spectroscopic and electrochemical results, are only weakly electronically coupled. Importantly, reduction of this complex by two electrons leads to the clean formation of N2O in quantitative yield. This complex therefore represents the first example of a functional model system for FNORs. The results provide key mechanistic insight into the mechanism of FNORs and, in particular, represent strong support for the proposed "super-reduced" mechanism for these enzymes.

  DOI：

  10.1021/ja309782m