octahydrobenzo[b]oxepin-2-one | 18335-60-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: octahydrobenzo[b]oxepin-2-one
• 英文别名: (5aS,9aR)-Octahydro-1-benzoxepin-2(3H)-one；(5aS,9aR)-4,5,5a,6,7,8,9,9a-octahydro-3H-benzo[b]oxepin-2-one
• CAS: 18335-60-9
• 化学式: C₁₀H₁₆O₂
• 分子量: 168.236
• InChiKey: JFTXZBPTXPXYOF-DTWKUNHWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  甲基三苯基溴化膦 、 octahydrobenzo[b]oxepin-2-one 在 sodium hydride 作用下， 以 二甲基亚砜 为溶剂， 反应 12.0h， 以24%的产率得到5-((1S,2R)-2-Hydroxy-cyclohexyl)-pentan-2-one
  参考文献：
  名称：

  非稳定化的叶立德with与内酯的反应

  摘要：

  中环内酯与亚甲基和亚烷基三苯基膦在二甲亚砜中的反应生成不饱和醇。

  DOI：

  10.1016/0040-4039(96)00698-3
• 作为产物：
  描述：

  trans-1-decalone 在 air 、 cyclohexanone monooxygenase 作用下， 生成 octahydro-benzo[c]oxepin-1-one 、 octahydrobenzo[b]oxepin-2-one 、 octahydrobenzo[b]oxepin-2-one
  参考文献：
  名称：

  Crystal Structures of Cyclohexanone Monooxygenase Reveal Complex Domain Movements and a Sliding Cofactor

  摘要：

  Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer-Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O-2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. We present here the atomic structures of CHMO from an environmental Rhodococcus strain bound with FAD and NADP(+) in two distinct states, to resolutions of 2.3 and 2.2 angstrom. The two conformations reveal domain shifts around multiple linkers and loop movements, involving conserved arginine 329 and tryptophan 492, which effect a translation of the nicotinamide resulting in a sliding cofactor. Consequently, the cofactor is ideally situated and subsequently repositioned during the catalytic cycle to first reduce the flavin and later stabilize formation of the Criegee intermediate. Concurrent movements of a loop adjacent to the active site demonstrate how this protein can effect large changes in the size and shape of the substrate binding pocket to accommodate a diverse range of substrates. Finally, the previously identified BVMO signature sequence is highlighted for its role in coordinating domain movements. Taken together, these structures provide mechanistic insights into CHMO-catalyzed Baeyer-Villiger oxidation.

  DOI：

  10.1021/ja9010578

文献信息

• Crystal Structures of Cyclohexanone Monooxygenase Reveal Complex Domain Movements and a Sliding Cofactor
  作者：I. Ahmad Mirza、Brahm J. Yachnin、Shaozhao Wang、Stephan Grosse、Hélène Bergeron、Akihiro Imura、Hiroaki Iwaki、Yoshie Hasegawa、Peter C. K. Lau、Albert M. Berghuis

  DOI：10.1021/ja9010578

  日期：2009.7.1

  Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer-Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O-2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. We present here the atomic structures of CHMO from an environmental Rhodococcus strain bound with FAD and NADP(+) in two distinct states, to resolutions of 2.3 and 2.2 angstrom. The two conformations reveal domain shifts around multiple linkers and loop movements, involving conserved arginine 329 and tryptophan 492, which effect a translation of the nicotinamide resulting in a sliding cofactor. Consequently, the cofactor is ideally situated and subsequently repositioned during the catalytic cycle to first reduce the flavin and later stabilize formation of the Criegee intermediate. Concurrent movements of a loop adjacent to the active site demonstrate how this protein can effect large changes in the size and shape of the substrate binding pocket to accommodate a diverse range of substrates. Finally, the previously identified BVMO signature sequence is highlighted for its role in coordinating domain movements. Taken together, these structures provide mechanistic insights into CHMO-catalyzed Baeyer-Villiger oxidation.
• Reaction of non stabilised phosphonium ylides with lactones
  作者：Yves Brunel、Gérard Rousseau

  DOI：10.1016/0040-4039(96)00698-3

  日期：1996.5

  Reaction of medium ring lactones with methylene and alkylidene triphenylphosphoranes in dimethyl sulfoxide led to unsaturated alcohols.

  中环内酯与亚甲基和亚烷基三苯基膦在二甲亚砜中的反应生成不饱和醇。