5-amino-4-chloro-2-(2,3-dihydroxy-phenyl)-2H-pyridazin-3-one | 50512-54-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: 5-amino-4-chloro-2-(2,3-dihydroxy-phenyl)-2H-pyridazin-3-one
• 英文别名: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)pyridazin-3(2H)-one；5-amino-4-chloro-2-(2,3-dihydroxyphenyl)pyridazin-3-one
• CAS: 50512-54-4
• 化学式: C₁₀H₈ClN₃O₃
• 分子量: 253.645
• InChiKey: NGWWIKMKDDRAOU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  17
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  99.2
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  5-amino-4-chloro-2-(2,3-dihydroxy-phenyl)-2H-pyridazin-3-one 、 氧气 生成 5-amino-4-chloro-2-(2-oxidomuconoyl)pyridazin-3(2H)-one(2-) 、 氢(+1)阳离子
  参考文献：
  名称：

  Muller R.; Haug S.; Eberspacher J., Hoppe Seylers Z Physiol Chem, 1977, 0018-4888, 797-805

  摘要：

  DOI：

文献信息

• Muller R.; Haug S.; Eberspacher J., Hoppe Seylers Z Physiol Chem, 1977, 0018-4888, 797-805
  作者：Muller R.、Haug S.、Eberspacher J.、Lingens F.

  DOI：——

  日期：——
• A Novel Non-heme Iron-Containing Dioxygenase
  作者：Rudolf MÜLLER、Stefan SCHMITT、Frdnz LINGENS

  DOI：10.1111/j.1432-1033.1982.tb06722.x

  日期：1982.7

  Previously we purified an enzyme from Phenylobacterium immobilis DSM 1986, which cleaves the catechol derivative of the herbicide Chloridazon [5‐amino‐4‐chloro‐2‐phenyl‐3(2H)‐pyridazinone] in the meta position. The enzyme, which could be crystallized, proved in Ouchterlony double‐diffusion tests to consist of a single protein species. No cross‐reaction was observed with other meta‐cleaving enzymes. Its light absorption spectrum showed a maximum at 279 nm (ɛ= 310 mM−1 cm−1), shoulders at 289 nm and 275 nm and a very weak band at around 430 nm (ɛ= 1.14 mM−1 cm−1). The amino acid analysis showed a slight excess of acidic amino acids, in agreement with the PI of 4.5.Surprisingly the enzyme per se is completely inactive, although it contains one non‐dialysable iron atom per subunit. It has to be activated by preincubation with ferrous ions or ascorbate. The enzyme activated this way is autoxidizable and returns to its non‐activated state in the presence of oxygen. During the reaction with the substrate, this inactivation seems to be enhanced about 100 times. Since this kind of activation and inactivation is not observed in other meta‐cleaving enzymes, this enzyme seems to represent a new type of a non‐heme iron dioxygenase. We tentatively propose the name Chloridazon‐catechol dioxygenase for this enzyme.