1-methyl-3-oxo-4-phenyl-cyclohexane-1,2-dicarboxylic acid diethyl ester | 854445-99-1

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 1-methyl-3-oxo-4-phenyl-cyclohexane-1,2-dicarboxylic acid diethyl ester
• 英文别名: 1-Methyl-3-oxo-4-phenyl-cyclohexan-1,2-dicarbonsaeure-diaethylester
• CAS: 854445-99-1
• 化学式: C₁₉H₂₄O₅
• 分子量: 332.397
• InChiKey: RAZMGTSUFWJLEW-UHFFFAOYSA-N

反应信息

• 作为反应物：
  描述：

  1-methyl-3-oxo-4-phenyl-cyclohexane-1,2-dicarboxylic acid diethyl ester 生成 (2-ethoxycarbonyl-2-methyl-6-oxo-5-phenyl-cyclohexyl)-acetic acid ethyl ester
  参考文献：
  名称：

  The Mo−OH proton of the low-pH form of sulfite oxidase: Comparison of the hyperfine interactions obtained from pulsed ENDOR, CW-EPR and ESEEM measurements

  摘要：

  Pulsed electron nuclear double resonance (ENDOR) spectra have been obtained for the exchangeable Mo-OH proton of the low-pH form of native chicken liver sulfite oxidase (SO) and recombinant human SO for the first time. The spectra of the two enzymes are very similar, indicating a similar binding geometry of the hydroxyl ligand to the Mo center. The isotropic hyperfine interaction (hfi) constant for the proton of the OH ligand in both enzymes is about 26 MHz. The anisotropic components of the hfi obtained from the pulsed ENDOR spectra are about 1.6-1.8 times larger than those obtained by continuous-wave electron paramagnetic resonance and electron spin echo envelope modulation. These hfi differences are explained by a rotational disorder of the Mo-OH group. A similar rotational disorder of the coordinated exchangeable ligand has been found previously for the high-pH and phosphate-inhibited forms of SO.

  DOI：

  10.1007/bf03166122
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 sodium 、 苯 作用下， 生成 1-methyl-3-oxo-4-phenyl-cyclohexane-1,2-dicarboxylic acid diethyl ester
  参考文献：
  名称：

  The Mo−OH proton of the low-pH form of sulfite oxidase: Comparison of the hyperfine interactions obtained from pulsed ENDOR, CW-EPR and ESEEM measurements

  摘要：

  Pulsed electron nuclear double resonance (ENDOR) spectra have been obtained for the exchangeable Mo-OH proton of the low-pH form of native chicken liver sulfite oxidase (SO) and recombinant human SO for the first time. The spectra of the two enzymes are very similar, indicating a similar binding geometry of the hydroxyl ligand to the Mo center. The isotropic hyperfine interaction (hfi) constant for the proton of the OH ligand in both enzymes is about 26 MHz. The anisotropic components of the hfi obtained from the pulsed ENDOR spectra are about 1.6-1.8 times larger than those obtained by continuous-wave electron paramagnetic resonance and electron spin echo envelope modulation. These hfi differences are explained by a rotational disorder of the Mo-OH group. A similar rotational disorder of the coordinated exchangeable ligand has been found previously for the high-pH and phosphate-inhibited forms of SO.

  DOI：

  10.1007/bf03166122