2-羟基-4-硝基苯酚 | 104959-69-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 中文名称: 2-羟基-4-硝基苯酚
• 英文名称: 2-hydroxy-4-nitrophenolate
• CAS: 104959-69-5
• 化学式: C₆H₄NO₄
• 分子量: 154.102
• InChiKey: XJNPNXSISMKQEX-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  11
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  89.1
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-羟基-4-硝基苯酚 在 (1+) 作用下， 以 高氯酸 为溶剂， 生成 p-nitro-o-benzoquinone 、 alkaline earth salt of/the/ methylsulfuric acid
  参考文献：
  名称：

  Herbert, John W.; Macartney, Donal H., Journal of the Chemical Society, Dalton Transactions, 1986, p. 1931 - 1936

  摘要：

  DOI：
• 作为产物：
  描述：

  4-硝基苯酚阴离子 、 氢(+1)阳离子 、 NADH 、 氧气 生成 2-羟基-4-硝基苯酚 、 水 、 nicotinamide adenine dinucleotide
  参考文献：
  名称：

  红球菌中4-硝基苯酚氧化的机理 菌株PN1：表征两种成分的4-硝基苯酚羟化酶及其表达。

  摘要：

  4-硝基苯酚（4-NP）是土壤中对硫磷等有机磷农药水解的有毒产物。红球菌 菌株PN1通过4-硝基邻苯二酚（4-NC）​​降解4-NP，用作唯一的碳，氮和能源。先前从PN1克隆的5kb EcoRI DNA片段包含一个参与4-NP氧化的基因簇（nphRA1A2）。通过序列分析，该基因簇有望编码AraC / XylS家族调节蛋白（NphR）和两组分4-NP羟化酶（NphA1和NphA2）。在红球菌菌株中的转录测定显示，在组成型表达的nphR存在下，nphA1的转录仅由4-NP（受测的几种酚类化合物）诱导。nphR的破坏取消了转录活性，表明nphR编码一种正调节蛋白。4-NP羟化酶的两个蛋白NphA1和NphA2在大肠杆菌中独立表达，并通过离子交换色谱法或亲和色谱法纯化。纯化的NphA2伴随着NADH的氧化还原黄素腺嘌呤二核苷酸（FAD），而纯化的NphA1在FAD，NADH和NphA2的存在下几

  DOI：

  10.1128/jb.00742-08

文献信息

• A Two-Component Monooxygenase Catalyzes Both the Hydroxylation of <i>p</i> -Nitrophenol and the Oxidative Release of Nitrite from 4-Nitrocatechol in <i>Bacillus sphaericus</i> JS905
  作者：Venkateswarlu Kadiyala、Jim C. Spain

  DOI：10.1128/aem.64.7.2479-2484.1998

  日期：1998.7

  Bacteria that metabolize p -nitrophenol (PNP) oxidize the substrate to 3-ketoadipic acid via either hydroquinone or 1,2,4-trihydroxybenzene (THB); however, initial steps in the pathway for PNP biodegradation via THB are unclear. The product of initial hydroxylation of PNP could be either 4-nitrocatechol or 4-nitroresorcinol. Here we describe the complete pathway for aerobic PNP degradation by Bacillus sphaericus JS905 that was isolated by selective enrichment from an agricultural soil in India. Washed cells of PNP-grown JS905 released nitrite in stoichiometric amounts from PNP and 4-nitrocatechol. Experiments with extracts obtained from PNP-grown cells revealed that the initial reaction is a hydroxylation of PNP to yield 4-nitrocatechol. 4-Nitrocatechol is subsequently oxidized to THB with the concomitant removal of the nitro group as nitrite. The enzyme that catalyzed the two sequential monooxygenations of PNP was partially purified and separated into two components by anion-exchange chromatography and size exclusion chromatography. Both components were required for NADH-dependent oxidative release of nitrite from PNP or 4-nitrocatechol. One of the components was identified as a reductase based on its ability to catalyze the NAD(P)H-dependent reduction of 2,6-dichlorophenolindophenol and nitroblue tetrazolium. Nitrite release from either PNP or 4-nitrocatechol was inhibited by the flavoprotein inhibitor methimazole. Our results indicate that the two monooxygenations of PNP to THB are catalyzed by a single two-component enzyme system comprising a flavoprotein reductase and an oxygenase.

  摘要 代谢 p -硝基苯酚（PNP）的细菌会通过对苯二酚或 1,2,4-三羟基苯（THB）将底物氧化为 3-酮基二酸；然而，通过 THB 对 PNP 进行生物降解的途径的初始步骤尚不清楚。PNP 最初羟基化的产物可能是 4-硝基邻苯二酚或 4-硝基间苯二酚。在这里，我们描述了由 芽孢杆菌 JS905 通过选择性富集从印度的农业土壤中分离出来。生长了 PNP 的 JS905 的洗涤细胞从 PNP 和 4-硝基邻苯二酚中释放出的亚硝酸盐达到了一定的数量。用从生长 PNP 的细胞中提取的提取物进行的实验表明，最初的反应是 PNP 发生羟基化反应，生成 4-硝基邻苯二酚。随后，4-硝基邻苯二酚被氧化成 THB，同时以亚硝酸盐的形式脱去硝基。通过阴离子交换色谱法和尺寸排阻色谱法，部分纯化了催化 PNP 两种连续单氧化作用的酶，并将其分离为两种成分。这两种成分都是依赖于 NADH 从 PNP 或 4-硝基儿茶酚中氧化释放亚硝酸盐所必需的。根据催化 2,6-二氯苯酚吲哚和硝基蓝四氮唑的 NAD(P)H 依赖性还原能力，确定其中一种成分为还原酶。黄素蛋白抑制剂甲巯咪唑可抑制 PNP 或 4-硝基邻苯二酚释放亚硝酸盐。我们的研究结果表明，从 PNP 到 THB 的两种单加氧作用是由黄素蛋白还原酶和加氧酶组成的单个双组分酶系统催化的。
• A Novel <i>p</i> -Nitrophenol Degradation Gene Cluster from a Gram-Positive Bacterium, <i>Rhodococcus opacus</i> SAO101
  作者：Wataru Kitagawa、Nobutada Kimura、Yoichi Kamagata

  DOI：10.1128/jb.186.15.4894-4902.2004

  日期：2004.8

  p -Nitrophenol (4-NP) is recognized as an environmental contaminant; it is used primarily for manufacturing medicines and pesticides. To date, several 4-NP-degrading bacteria have been isolated; however, the genetic information remains very limited. In this study, a novel 4-NP degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101, was identified and characterized. The deduced amino acid sequences of npcB , npcA , and npcC showed identity with phenol 2-hydroxylase component B (reductase, PheA2) of Geobacillus thermoglucosidasius A7 (32%), with 2,4,6-trichlorophenol monooxygenase (TcpA) of Ralstonia eutropha JMP134 (44%), and with hydroxyquinol 1,2-dioxygenase (ORF2) of Arthrobacter sp. strain BA-5-17 (76%), respectively. The npcB , npcA , and npcC genes were cloned into pET-17b to construct the respective expression vectors pETnpcB, pETnpcA, and pETnpcC. Conversion of 4-NP was observed when a mixture of crude cell extracts of Escherichia coli containing pETnpcB and pETnpcA was used in the experiment. The mixture converted 4-NP to hydroxyquinol and also converted 4-nitrocatechol (4-NCA) to hydroxyquinol. Furthermore, the crude cell extract of E. coli containing pETnpcC converted hydroxyquinol to maleylacetate. These results suggested that npcB and npcA encode the two-component 4-NP/4-NCA monooxygenase and that npcC encodes hydroxyquinol 1,2-dioxygenase. The npcA and npcC mutant strains, SDA1 and SDC1, completely lost the ability to grow on 4-NP as the sole carbon source. These results clearly indicated that the cloned npc genes play an essential role in 4-NP mineralization in R. opacus SAO101.

  摘要 p -硝基苯酚（4-NP）被认为是一种环境污染物，主要用于制造药物和杀虫剂。迄今为止，已分离出几种降解 4-NP 的细菌，但遗传信息仍然非常有限。本研究从一种革兰氏阳性细菌中发现了一个新的 4-NP 降解基因簇、 乳清红球菌 SAO101 中的一个新型 4-NP 降解基因簇。推导出了 npcB , npcA 和 npcC 与热葡糖苷酸革囊菌的苯酚 2-羟化酶 B 组份（还原酶，PheA2）显示出相同性 与 2,4,6-三羟基苯酚还原酶 B 组份（还原酶，PheA2）的同一性。 的 2,4,6-三氯苯酚单加氧酶（TcpA）的同一性。 的 2,4,6-三氯苯酚单加氧酶（TcpA JMP134（44%），以及羟基喹啉 1,2-二氧 化酶（ORF2） 节杆菌 菌株 BA-5-17 的羟基对苯二酚 1,2-二氧化酶（ORF2）（76%）。在 npcB , npcA 和 npcC 基因克隆到 pET-17b 中，分别构建表达载体 pETnpcB、pETnpcA 和 pETnpcC。当大肠杆菌的粗细胞提取物与 4-NP 的混合物混合时，可观察到 4-NP 的转化。 大肠杆菌 在实验中使用含有 pETnpcB 和 pETnpcA 的大肠杆菌粗细胞提取物混合物时，观察到了 4-NP 的转化。该混合物将 4-NP 转化为羟基苯酚，还将 4-硝基邻苯二酚（4-NCA）转化为羟基苯酚。此外，大肠杆菌的粗细胞提取物 大肠杆菌 含有 pETnpcC 的大肠杆菌细胞提取物将羟基苯酚转化为马来乙酸酯。这些结果表明 npcB 和 npcA 编码双组分 4-NP/4-NCA 单加氧酶，而 npcC 编码羟基喹啉 1,2-二氧合酶。npcA npcA 和 npcC 突变株 SDA1 和 SDC1 完全丧失了以 4-NP 为唯一碳源的生长能力。这些结果清楚地表明，克隆的 npc 基因在 4-NP 矿化过程中发挥了重要作用。 R. opacus SAO101。
• Molecular Characterization and Substrate Specificity of Nitrobenzene Dioxygenase from <i>Comamonas</i> sp. Strain JS765
  作者：Daniel J. Lessner、Glenn R. Johnson、Rebecca E. Parales、Jim C. Spain、David T. Gibson

  DOI：10.1128/aem.68.2.634-641.2002

  日期：2002.2

  Comamonas sp. strain JS765 can grow with nitrobenzene as the sole source of carbon, nitrogen, and energy. We report here the sequence of the genes encoding nitrobenzene dioxygenase (NBDO), which catalyzes the first step in the degradation of nitrobenzene by strain JS765. The components of NBDO were designated Reductase _NBZ , Ferredoxin _NBZ , Oxygenase _NBZα , and Oxygenase _NBZβ , with the gene designations nbzAa , nbzAb , nbzAc , and nbzAd , respectively. Sequence analysis showed that the components of NBDO have a high level of homology with the naphthalene family of Rieske nonheme iron oxygenases, in particular, 2-nitrotoluene dioxygenase from Pseudomonas sp. strain JS42. The enzyme oxidizes a wide range of substrates, and relative reaction rates with partially purified Oxygenase _NBZ revealed a preference for 3-nitrotoluene, which was shown to be a growth substrate for JS765. NBDO is the first member of the naphthalene family of Rieske nonheme iron oxygenases reported to oxidize all of the isomers of mono- and dinitrotoluenes with the concomitant release of nitrite.

  摘要 Comamonas 菌株 JS765 能以硝基苯作为唯一的碳、氮和能量来源进行生长。我们在此报告了编码硝基苯二氧酶（NBDO）的基因序列，该酶催化了 JS765 菌株降解硝基苯的第一步。NBDO 的组分被命名为还原酶 NBZ 铁氧化还原酶 NBZ 氧化酶 NBZα 和氧化酶 NBZβ ，基因名称为 nBZAa , nBZAb , nBZAc 和 nBZAd 和 nBZAd。序列分析表明，NBDO 的组成成分与萘家族的里斯克非血红素铁氧合酶，特别是假单胞菌中的 2-硝基甲苯二氧合酶，具有高度的同源性。 假单胞菌 菌株 JS42 的 2-硝基甲苯二氧酶。该酶可氧化多种底物，与部分纯化的加氧酶的相对反应速率如下 NBZ 的相对反应速率显示，该酶偏好 3-硝基甲苯，而 3-硝基甲苯被证明是 JS765 的生长底物。据报道，NBDO 是萘系里斯克非血红素铁氧合酶家族的第一个成员，它能氧化一硝基甲苯和二硝基甲苯的所有异构体，同时释放亚硝酸盐。
• Mitra D.; Vaidyanathan C.S., Biochem Int, 1984, 0158-5231, 609-15
  作者：Mitra D.、Vaidyanathan C.S.

  DOI：——

  日期：——
• Both Cytochromes P450 2E1 and 3A Are Involved in the O-Hydroxylation of <i>p</i>-Nitrophenol, a Catalytic Activity Known To Be Specific for P450 2E1
  作者：Alain Zerilli、Damrong Ratanasavanh、Danièle Lucas、Thierry Goasduff、Yvonne Dréano、Christophe Menard、Daniel Picart、François Berthou

  DOI：10.1021/tx970048z

  日期：1997.10.1

  4-Nitrophenol 2-hydroxylation activity was previously shown to be mainly catalyzed by P450 2E1 in animal species and humans. As this chemical compound is widely used as an in vitro probe for P450 2E1, this study was carried out to test its catalytic specificity. First, experiments were carried out on liver microsomes and hepatocyte cultures of rat treated with different inducers. Liver microsomes from pyrazole-and dexamethasone-treated rats hydroxylated p-nitrophenol with a metabolic rate increased by 2.5- and 2.7-fold vs control. Dexamethasone treatment increased the hepatic content of P450 3A but not that of P450 2E1. Two specific inhibitors of P450 3A catalytic activities, namely, ketoconazole and troleandomycin (TAO), inhibited up to 50% of 4-nitrophenol hydroxylation in dexamethasone-treated rats but not in controls. Hepatocyte cultures from dexamethasone-treated rats transformed p-nitrophenol into 4-nitrocatechol 7.8 times more than controls. This catalytic activity was inhibited by TAO. Similarly, hepatocyte cultures from pyrazole-treated rats hydroxylated p-nitrophenol with a metabolic ratio increased by about 8-fold vs control. This reaction was inhibited by diethyl dithiocarbamate and dimethyl sulfoxide, both inhibitors of P450 2E1. Second, the capability of human P450s other than P450 2E1 to catalyze the formation of 4-nitrocatechol was examined in a panel of 13 human liver microsomes. Diethyl dithiocarbamate and ketoconazole reduced 4-nitrophenol hydroxylase activity by 77% (+/-11) and 13% (+/-16), respectively. Furthermore, the residual activity following diethyl dithiocarbamate inhibition was significantly correlated with seven P450 3A4 catalytic activities. Finally, the use of human cell lines genetically engineered for expression of human P450s demonstrated that P450 2E1 and 3A4 hydroxylated 4-nitrophenol with turnovers of 19.5 and 1.65 min(-1), respectively. In conclusion, P450 3A may make a significant contribution to 4-nitrophenol hydroxylase activity in man and rat.