tetrakis(bipyridyl)(μ-peroxo)(μ-hydroxo)dicobalt(III) | 83897-67-0

• 英文名称: tetrakis(bipyridyl)(μ-peroxo)(μ-hydroxo)dicobalt(III)
• CAS: 83897-67-0
• 化学式: C₄₀H₃₃Co₂N₈O₃
• 分子量: 791.74
• InChiKey: BAOGSYYCMNIACX-UHFFFAOYSA-N

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

• 作为产物：
  描述：

  Co(2,2'-bipyridine)(2+) 在 氢氧化钾 、 氧气 作用下， 以 甲醇 、 水 为溶剂， 生成 tetrakis(bipyridyl)(μ-peroxo)(μ-hydroxo)dicobalt(III)
  参考文献：
  名称：

  Bedell, Stephen A.; Martell, Arthur E., Inorganic Chemistry, 1983, vol. 22, # 2, p. 364 - 367

  摘要：

  DOI：

文献信息

• Characterization and evaluation of photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)cobalt caged oxygen compounds to facilitate time-resolved crystallographic studies of cytochrome c oxidase
  作者：Emil Sandelin、Jonatan Johannesson、Ola Wendt、Gisela Brändén、Richard Neutze、Carl-Johan Wallentin

  DOI：10.1007/s43630-024-00558-x

  日期：2024.5

  Photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)-cobalt-based caged oxygen compounds have been synthesized and characterized by optical absorbance spectroscopy, X-ray crystallography. and the quantum yield and redox stability were investigated. Furthermore, conditions were established where redox incompatibilities encountered between caged oxygen compounds and oxygen-dependant cytochrome c oxidase (CcO) could be circumvented. Herein, we demonstrate that millimolar concentrations of molecular oxygen can be released from a caged oxygen compound with spatio-temporal control upon laser excitation, triggering enzymatic turnover in cytochrome c oxidase. Spectroscopic evidence confirms the attainment of a homogeneous reaction initiation at concentrations and conditions relevant for further crystallography studies. This was demonstrated by the oxidizing microcrystals of reduced CcO by liberation of millimolar concentrations of molecular oxygen from a caged oxygen compound. We believe this will expand the scope of available techniques for the detailed investigation of oxygen-dependant enzymes with its native substrate and facilitate further time-resolved X-ray based studies such as wide/small angle X-ray scattering and serial femtosecond crystallography. Graphical abstract