2-[4,11-dimethyl-8-(2-methylsulfanylethyl)-1,4,8,11-tetrazacyclotetradec-1-yl]ethanethiolate;nickel(2+);trifluoromethanesulfonate | 1370087-66-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磺酸及其衍生物
• 英文名称: 2-[4,11-dimethyl-8-(2-methylsulfanylethyl)-1,4,8,11-tetrazacyclotetradec-1-yl]ethanethiolate;nickel(2+);trifluoromethanesulfonate
• CAS: 1370087-66-3
• 化学式: CF₃O₃S*C₁₇H₃₇N₄NiS₂
• 分子量: 569.4
• InChiKey: WDKAGTKPRYIOSO-UHFFFAOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  1.21
• 重原子数：
  32
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  105
• 氢给体数：
  0
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  [Ni(1,8-bis(2-methylthioethyl)-4,11-dimethyl-1,4,8,11-tetraazatetradecane)](OTf) 在 2,6-dimesitylphenylSH 作用下， 以 四氢呋喃 为溶剂， 以21%的产率得到2-[4,11-dimethyl-8-(2-methylsulfanylethyl)-1,4,8,11-tetrazacyclotetradec-1-yl]ethanethiolate;nickel(2+);trifluoromethanesulfonate
  参考文献：
  名称：

  Model Studies of Methyl CoM Reductase: Methane Formation via CH₃–S Bond Cleavage of Ni(I) Tetraazacyclic Complexes Having Intramolecular Methyl Sulfide Pendants

  摘要：

  The Ni(I) tetraazacycles [Ni(dmmtc)](+) and [Ni(mtc)](+), which have methylthioethyl pendants, were synthesized as models of the reduced state of the active site of methyl coenzyme M reductase (MCR), and their structures and redox properties were elucidated (dmmtc, 1,8-dimethyl-4,11-bis{(2-methylthio)ethyl}-1,4,8,11-tetraaza-1,4,8,11-cyclotetradecane; mtc, 1,8-{bis(2-methylthio)ethyl}-1,4,8,11-tetraaza-1,4,8,11-cyclotetradecane). The intramolecular CH3-S bond of the thioether pendant of [Ni-I(dmmtc)](OTf) was cleaved in THF at 75 degrees C in the presence of the bulky thiol DmpSH, which acts as a proton source, and methane was formed in 31% yield and a Ni(II) thiolate complex was concomitantly obtained (Dmp = 2,6-dimesityphenyl). The CH3-S bond cleavage of [Ni-I(mtc)](+) also proceeded similarly, but under milder conditions probably due to the lower potential of the [Ni-I(mtc)](+) complex. These results indicate that the robust CH3-S bond can be homolytically cleaved by the Ni(I) center when they are properly arranged, which highlights the significance of the F430 Ni environment in the active site of the MCR protein.

  DOI：

  10.1021/ic300017k