(2-oxocyclohexane-1,3,5-triylidene)tris(azinate) | 730918-86-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (2-oxocyclohexane-1,3,5-triylidene)tris(azinate)
• CAS: 730918-86-2
• 化学式: C₆H₄N₃O₇
• 分子量: 230.114
• InChiKey: INFUDYKBMBQVDH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  16.0
• 可旋转键数：
  0.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  164.46
• 氢给体数：
  0.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  (2-oxocyclohexane-1,3,5-triylidene)tris(azinate) 在 Tris-HCl buffer 作用下， 生成
  参考文献：
  名称：

  摘要：

  Initial F-420-dependent hydrogenation of 2,4,6-trinitrophenol (picric acid) generated the hydride sigma-complex of picrate and finally the dihydride complex. With 2,4-dinitrophenol the hydride sigma-complex of 2,4-dinitrophenol is generated. The hydride transferring enzyme system showed activity against several substituted 2,4-dinitrophenols but not with mononitrophenols. A K-m-value of 0.06 mM of the hydride transfer for picrate as substrate was found. The pH optima of the NADPH-dependent F-420 reductase and for the hydride transferase were 5.5 and 7.5, respectively. An enzymatic activity has been identified catalyzing the release of stoichometric amounts of I mol nitrite from 1 mol of the dihydride sigma-complex of picrate. This complex was synthesized by chemical reduction of picrate and characterized by H-1 and C-13 NMR spectroscopy. The hydride sigma-complex of 2,4-dinitrophenol has been identified as the denitration product. The nitrite-eliminating activity was enriched and clearly separated from the hydride transferring enzyme system by FPLC. 2,4-Dinitrophenol has been disproven as a metabolite of picrate (Ebert et al. 1999) and a convergent catabolic pathway for picrate and 2,4-dinitrophenol with the hydride sigma-complex of 2,4-dinitrophenol as the common intermediate has been demonstrated.

  DOI：

  10.1023/a:1014447700775
• 作为产物：
  描述：

  2,4,6-三硝基苯酚阴离子 在 还原型辅酶II(NADPH)四钠盐 F₄₂₀ reductase 、 coenzyme F₄₂₀ 、 hydride transferase 作用下， 生成 (2-oxocyclohexane-1,3,5-triylidene)tris(azinate)
  参考文献：
  名称：

  摘要：

  Initial F-420-dependent hydrogenation of 2,4,6-trinitrophenol (picric acid) generated the hydride sigma-complex of picrate and finally the dihydride complex. With 2,4-dinitrophenol the hydride sigma-complex of 2,4-dinitrophenol is generated. The hydride transferring enzyme system showed activity against several substituted 2,4-dinitrophenols but not with mononitrophenols. A K-m-value of 0.06 mM of the hydride transfer for picrate as substrate was found. The pH optima of the NADPH-dependent F-420 reductase and for the hydride transferase were 5.5 and 7.5, respectively. An enzymatic activity has been identified catalyzing the release of stoichometric amounts of I mol nitrite from 1 mol of the dihydride sigma-complex of picrate. This complex was synthesized by chemical reduction of picrate and characterized by H-1 and C-13 NMR spectroscopy. The hydride sigma-complex of 2,4-dinitrophenol has been identified as the denitration product. The nitrite-eliminating activity was enriched and clearly separated from the hydride transferring enzyme system by FPLC. 2,4-Dinitrophenol has been disproven as a metabolite of picrate (Ebert et al. 1999) and a convergent catabolic pathway for picrate and 2,4-dinitrophenol with the hydride sigma-complex of 2,4-dinitrophenol as the common intermediate has been demonstrated.

  DOI：

  10.1023/a:1014447700775

文献信息

• ——
  作者：Sybille Ebert、Peter Fischer、Hans-Joachim Knackmuss

  DOI：10.1023/a:1014447700775

  日期：——

  Initial F-420-dependent hydrogenation of 2,4,6-trinitrophenol (picric acid) generated the hydride sigma-complex of picrate and finally the dihydride complex. With 2,4-dinitrophenol the hydride sigma-complex of 2,4-dinitrophenol is generated. The hydride transferring enzyme system showed activity against several substituted 2,4-dinitrophenols but not with mononitrophenols. A K-m-value of 0.06 mM of the hydride transfer for picrate as substrate was found. The pH optima of the NADPH-dependent F-420 reductase and for the hydride transferase were 5.5 and 7.5, respectively. An enzymatic activity has been identified catalyzing the release of stoichometric amounts of I mol nitrite from 1 mol of the dihydride sigma-complex of picrate. This complex was synthesized by chemical reduction of picrate and characterized by H-1 and C-13 NMR spectroscopy. The hydride sigma-complex of 2,4-dinitrophenol has been identified as the denitration product. The nitrite-eliminating activity was enriched and clearly separated from the hydride transferring enzyme system by FPLC. 2,4-Dinitrophenol has been disproven as a metabolite of picrate (Ebert et al. 1999) and a convergent catabolic pathway for picrate and 2,4-dinitrophenol with the hydride sigma-complex of 2,4-dinitrophenol as the common intermediate has been demonstrated.