7-methyl-N(10)-isobutylisoalloxazine | 649763-46-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 蝶啶及其衍生物
• 英文名称: 7-methyl-N(10)-isobutylisoalloxazine
• 英文别名: 7-Methyl-10-(2-methylpropyl)benzo[g]pteridine-2,4(3H,10H)-dione；7-methyl-10-(2-methylpropyl)benzo[g]pteridine-2,4-dione
• CAS: 649763-46-2
• 化学式: C₁₅H₁₆N₄O₂
• 分子量: 284.318
• InChiKey: QISVDKGJESEOGC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  21
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  74.1
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  2-methyl-N-(4-methyl-2-nitrophenyl)propanamide 在 boron trioxide 、 palladium on activated charcoal 、 lithium aluminium tetrahydride 、 氢气 、 ammonium formate 、 溶剂黄146 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 3.67h， 生成 7-methyl-N(10)-isobutylisoalloxazine
  参考文献：
  名称：

  Model Systems for Flavoenzyme Activity:  Relationships between Cofactor Structure, Binding and Redox Properties

  摘要：

  A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E-1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.

  DOI：

  10.1021/ja036940b

文献信息

• Model Systems for Flavoenzyme Activity:  Relationships between Cofactor Structure, Binding and Redox Properties
  作者：Yves-Marie Legrand、Mark Gray、Graeme Cooke、Vincent M. Rotello

  DOI：10.1021/ja036940b

  日期：2003.12.1

  A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E-1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.