[Os(4,4'-dimethyl-2,2'-bipyridine)2Cl2]Cl | 238759-94-9

• 英文名称: [Os(4,4'-dimethyl-2,2'-bipyridine)2Cl2]Cl
• 英文别名: [Os(dm-bpy)2Cl2]Cl
• CAS: 238759-94-9
• 化学式: C₂₄H₂₄Cl₂N₄Os*Cl
• 分子量: 665.04
• InChiKey: GZPJDOITXCSTLJ-UHFFFAOYSA-K

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：

  [Os(4,4'-dimethyl-2,2'-bipyridine)2Cl2]Cl 在 sodium dithionite 作用下， 以 甲醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 生成 osmium(II) bis(4,4'-dimethyl-2,2'-bipyridine) dichloride
  参考文献：
  名称：

  Kinetics of Redox Polymer-Mediated Enzyme Electrodes

  摘要：

  Oxygen-reducing enzyme electrodes are prepared from laccase of Trametes versicolor and a series of osmium-based redox polymer mediators covering a range of redox potentials from 0.11 to 0.85 V. Experimentally obtained current density generated by the film electrodes is analyzed using a one-dimensional numerical model to obtain kinetic parameters. The bimolecular rate constant for mediation is found to vary with mediator redox potential from 250 s(-1) M-1 when mediator and enzyme are close in redox potential to 9.4 x 10(4) s(-1) M-1 when the redox potential difference is large. The value of the bimolecular rate constant for the simultaneously occurring laccase-oxygen reaction is found to be 2.4 x 10(-5) s(-1) M-1. The relationship between mediator-enzyme overpotential and bimolecular rate constant is used to determine the optimum mediator redox potential for maximum power output of a hypothetical biofuel cell with a planar cathode and a reversible hydrogen anode. For laccase of T. versicolor (E-e(o) = 0.82), the optimum mediator potential is 0.66 V (SHE), and a molecular structure is presented to achieve this result.

  DOI：

  10.1021/ja0781543
• 作为产物：
  描述：

  4,4'-二甲基-2,2'-联吡啶 、 potassium hexachloroosmate(IV) 以 N,N-二甲基甲酰胺 为溶剂， 生成 [Os(4,4'-dimethyl-2,2'-bipyridine)2Cl2]Cl
  参考文献：
  名称：

  Kinetics of Redox Polymer-Mediated Enzyme Electrodes

  摘要：

  Oxygen-reducing enzyme electrodes are prepared from laccase of Trametes versicolor and a series of osmium-based redox polymer mediators covering a range of redox potentials from 0.11 to 0.85 V. Experimentally obtained current density generated by the film electrodes is analyzed using a one-dimensional numerical model to obtain kinetic parameters. The bimolecular rate constant for mediation is found to vary with mediator redox potential from 250 s(-1) M-1 when mediator and enzyme are close in redox potential to 9.4 x 10(4) s(-1) M-1 when the redox potential difference is large. The value of the bimolecular rate constant for the simultaneously occurring laccase-oxygen reaction is found to be 2.4 x 10(-5) s(-1) M-1. The relationship between mediator-enzyme overpotential and bimolecular rate constant is used to determine the optimum mediator redox potential for maximum power output of a hypothetical biofuel cell with a planar cathode and a reversible hydrogen anode. For laccase of T. versicolor (E-e(o) = 0.82), the optimum mediator potential is 0.66 V (SHE), and a molecular structure is presented to achieve this result.

  DOI：

  10.1021/ja0781543