1,2-dihydro-1,2-dihydroxy-dibenzofuran

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并呋喃
• 英文名称: 1,2-dihydro-1,2-dihydroxy-dibenzofuran
• 英文别名: 1,2-Dihydroxy-1,2-dihydrodibenzofuran；1,2-dihydrodibenzofuran-1,2-diol
• 化学式: C₁₂H₁₀O₃
• 分子量: 202.21
• InChiKey: SFFBNOAHWBDWNL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  15
• 可旋转键数：
  0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  53.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  二苯并呋喃 在 His-tagged oxygenase BphAE(RR₄₁) 、 氧气 、 还原型辅酶Ⅰ 作用下， 生成 1,2-dihydro-1,2-dihydroxy-dibenzofuran 、 3,4-dihydro-3,4-dihydroxy-dibenzofuran
  参考文献：
  名称：

  Retuning Rieske-type Oxygenases to Expand Substrate Range

  摘要：

  Rieske-type oxygenases are promising biocatalysts for the destruction of persistent pollutants or for the synthesis of fine chemicals. In this work, we explored pathways through which Rieske-type oxygenases evolve to expand their substrate range. BphAE(p4), a variant biphenyl dioxygenase generated from Burkholderia xenovorans LB400 BphAE(LB400) by the double substitution T335A/F336M, and BphAE(RR41), obtained by changing Asn(338), Ile(341), and Leu(409) of BphAEp(4) to Gln(338), Val(341), and Phe(409), metabolize dibenzofuran two and three times faster than BphAE(LB400), respectively. Steady-state kinetic measurements of single-and multiple-substitution mutants of BphAE(LB400) showed that the single T335A and the double N338Q/L409F substitutions contribute significantly to enhanced catalytic activity toward dibenzofuran. Analysis of crystal structures showed that the T335A substitution relieves constraints on a segment lining the catalytic cavity, allowing a significant displacement in response to dibenzofuran binding. The combined N338Q/L409F substitutions alter substrate-induced conformational changes of protein groups involved in subunit assembly and in the chemical steps of the reaction. This suggests a responsive induced fit mechanism that retunes the alignment of protein atoms involved in the chemical steps of the reaction. These enzymes can thus expand their substrate range through mutations that alter the constraints or plasticity of the catalytic cavity to accommodate new substrates or that alter the induced fit mechanism required to achieve proper alignment of reaction-critical atoms or groups.

  DOI：

  10.1074/jbc.m111.255174

文献信息

• Oxygenation Reactions of Various Tricyclic Fused Aromatic Compounds Using Escherichia coli and Streptomyces lividans Transformants Carrying Several Arene Dioxygenase Genes
  作者：Kazutoshi SHINDO、Yasuo OHNISHI、Hyo-Kon CHUN、Haruko TAKAHASHI、Miki HAYASHI、Atsushi SAITO、Kazuo IGUCHI、Kensuke FURUKAWA、Shigeaki HARAYAMA、Sueharu HORINOUCHI、Norihiko MISAWA

  DOI：10.1271/bbb.65.2472

  日期：2001.1

  compounds), including various tricyclic fused aromatic compounds such as fluorene, dibenzofuran, dibenzothiophene, carbazole, acridene, and phenanthridine, were done using the cells of Escherichia coli transformants expressing several arene dioxygenase genes. E. coli carrying the phenanthrene dioxygenase (phdABCD) genes derived from the marine bacterium Nocardioides sp. strain KP7 converted all of these

  使用表达几种芳烃双加氧酶基因的大肠杆菌转化子的细胞，对包括各种三环稠合芳族化合物（例如芴，二苯并呋喃，二苯并噻吩，咔唑，a啶和菲啶）在内的芳烃（芳族化合物）进行了生物转化（生物转化）实验。带有从海洋细菌Nocardioides sp。衍生的菲双加氧酶（phdABCD）基因的大肠杆菌。菌株KP7转化了所有这些三环芳族化合物，而带有恶臭假单胞菌F1甲苯双加氧酶（todC1C2BA）基因或假拟疟原虫KF707联苯双加氧酶（bphA1A2A3A4）基因的大肠杆菌无法转化这些底物。出乎意料的是，大肠杆菌携带杂种双加氧酶（todC1 ::: 在甲苯和联苯双加氧酶之间具有亚基取代的bphA2A3A4）基因能够转化芴，二苯并呋喃和二苯并噻吩。还评估了携带菲双加氧酶基因的淡紫色链霉菌转化体的细胞对各种三环稠合芳族化合物的生物转化。该放线菌转化的能力与携带相应基因的大肠杆菌相似。用这些重组细菌细胞从芳香族化合
• Retuning Rieske-type Oxygenases to Expand Substrate Range
  作者：Mahmood Mohammadi、Jean-François Viger、Pravindra Kumar、Diane Barriault、Jeffrey T. Bolin、Michel Sylvestre

  DOI：10.1074/jbc.m111.255174

  日期：2011.8

  Rieske-type oxygenases are promising biocatalysts for the destruction of persistent pollutants or for the synthesis of fine chemicals. In this work, we explored pathways through which Rieske-type oxygenases evolve to expand their substrate range. BphAE(p4), a variant biphenyl dioxygenase generated from Burkholderia xenovorans LB400 BphAE(LB400) by the double substitution T335A/F336M, and BphAE(RR41), obtained by changing Asn(338), Ile(341), and Leu(409) of BphAEp(4) to Gln(338), Val(341), and Phe(409), metabolize dibenzofuran two and three times faster than BphAE(LB400), respectively. Steady-state kinetic measurements of single-and multiple-substitution mutants of BphAE(LB400) showed that the single T335A and the double N338Q/L409F substitutions contribute significantly to enhanced catalytic activity toward dibenzofuran. Analysis of crystal structures showed that the T335A substitution relieves constraints on a segment lining the catalytic cavity, allowing a significant displacement in response to dibenzofuran binding. The combined N338Q/L409F substitutions alter substrate-induced conformational changes of protein groups involved in subunit assembly and in the chemical steps of the reaction. This suggests a responsive induced fit mechanism that retunes the alignment of protein atoms involved in the chemical steps of the reaction. These enzymes can thus expand their substrate range through mutations that alter the constraints or plasticity of the catalytic cavity to accommodate new substrates or that alter the induced fit mechanism required to achieve proper alignment of reaction-critical atoms or groups.