4-甲基-5-硝基邻苯二酚 | 68906-21-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 中文名称: 4-甲基-5-硝基邻苯二酚
• 中文别名: 4-甲基-5-硝基CATECHOL
• 英文名称: 4-methyl-5-nitrobenzene-1,2-diol
• 英文别名: 4-methyl-5-nitrocatechol；4-methyl-5-nitro-pyrocatechol；4-Methyl-5-nitro-brenzcatechin；6-Nitro-3.4-dioxy-toluol；6-Nitro-3.4-dioxy-1-methyl-benzol
• CAS: 68906-21-8
• 化学式: C₇H₇NO₄
• mdl: MFCD04039616
• 分子量: 169.137
• InChiKey: WLLRAKCRHPMKNA-UHFFFAOYSA-N

物化性质

• 熔点：
  180-182°C
• 沸点：
  354.5±42.0 °C(Predicted)
• 密度：
  1.478
• 溶解度：
  可溶于氯仿（轻微，超声），乙酸乙酯（轻微），甲醇（轻微）

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.142
• 拓扑面积：
  86.3
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 危险性防范说明：
  P261,P264,P270,P271,P280,P301+P312,P302+P352,P304+P340,P330,P363,P501
• 危险性描述：
  H302,H312,H332

反应信息

• 作为反应物：
  描述：

  4-甲基-5-硝基邻苯二酚 在 吡啶 、 双氧水 、 potassium hexacyanoferrate(III) 作用下， 以 水 为溶剂， 生成
  参考文献：
  名称：

  仿生条件下神经毒素6-硝基多巴胺及相关4-硝基邻苯二酚的氧化

  摘要：

  在0.05 M磷酸盐缓冲液（pH 7.4 ）中用辣根过氧化物酶（HRP）/ H 2 O 2氧化6-硝基多巴胺（1），作为主要产物，新的5- [4-（2-氨基乙基）-2-羟基-5-硝基苯氧基] -6，7-二羟基-4-硝基-2，3-二氢吲哚（4）。4 nitrocatechols的类似氧化2和3与HRP / H 2 ö 2或K 3的Fe（CN）6，得到主要是二聚体5 / 6和7 / 8。这些产物可能是通过4-硝基-o产生的-醌或4-硝基-2,3-二氢吲哚-6,7-二酮中间体，被中间体硝基邻苯二酚捕获。

  DOI：

  10.1016/s0040-4020(00)00483-x
• 作为产物：
  描述：

  3,4-二羟基甲苯 在 sodium nitrite 、 硫酸 作用下， 以 水 为溶剂， 生成 4-甲基-5-硝基邻苯二酚
  参考文献：
  名称：

  大气相关硝基儿茶酚的气相红外截面和单晶结构数据

  摘要：

  使用 ESC-Q-UAIC（由石英制成的环境模拟室）评估 3-硝基儿茶酚、5-甲基-3-硝基儿茶酚、4-硝基儿茶酚和 4-甲基-5-硝基儿茶酚的气相红外吸收截面罗马尼亚雅西的“Alexandru Ioan Cuza”大学）光反应器设施。650–4000 cm - 1范围内的特定红外吸收和积分带强度用长程气相 FT-IR 技术研究。在这些研究中使用了两种不同的硝基儿茶酚加入反应器的方法（固体和液体转移方法）。除了传统的核磁共振 (NMR) 和红外 (IR) 光谱之外，所有研究的硝基儿茶酚都被合成并通过 X 射线衍射光谱技术表征，以评估它们在气相和固相中的结构-性质关系。本研究首次报告了（甲基）硝基儿茶酚的气相红外截面和 X 射线衍射分析。

  DOI：

  10.1016/j.saa.2021.120379

文献信息

• 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase
  作者：W C Suen、B E Haigler、J C Spain

  DOI：10.1128/jb.178.16.4926-4934.1996

  日期：1996.8

  2,4-Dinitrotoluene (DNT) dioxygenase from Burkholderia sp. strain DNT catalyzes the initial oxidation of DNT to form 4-methyl-5-nitrocatechol (MNC) and nitrite. The displacement of the aromatic nitro group by dioxygenases has only recently been described, and nothing is known about the evolutionary origin of the enzyme systems that catalyze these reactions. We have shown previously that the gene encoding DNT dioxygenase is localized on a degradative plasmid within a 6.8-kb NsiI DNA fragment (W.-C. Suen and J. C. Spain, J. Bacteriol. 175:1831-1837, 1993). We describe here the sequence analysis and the substrate range of the enzyme system encoded by this fragment. Five open reading frames were identified, four of which have a high degree of similarity (59 to 78% identity) to the components of naphthalene dioxygenase (NDO) from Pseudomonas strains. The conserved amino acid residues within NDO that are involved in cofactor binding were also identified in the gene encoding DNT dioxygenase. An Escherichia coli clone that expressed DNT dioxygenase converted DNT to MNC and also converted naphthalene to (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. In contrast, the E. coli clone that expressed NDO did not oxidize DNT. Furthermore, the enzyme systems exhibit similar broad substrate specificities and can oxidize such compounds as indole, indan, indene, phenetole, and acenaphthene. These results suggest that DNT dioxygenase and the NDO enzyme system share a common ancestor.

  Burkholderia sp.菌株DNT的2,4-二硝基甲苯（DNT）双氧酶催化DNT的初始氧化，形成4-甲基-5-硝基邻苯二酚（MNC）和亚硝酸盐。芳香族硝基被双氧酶取代的反应最近才被描述，关于催化这些反应的酶系统的进化起源一无所知。我们之前已经表明，编码DNT双氧酶的基因定位于一个降解质粒上，位于一个6.8-kb NsiI DNA片段内（W.-C. Suen和J.C. Spain，J. Bacteriol. 175:1831-1837，1993年）。在本文中，我们描述了这个片段编码的酶系统的序列分析和底物范围。鉴定了五个开放阅读框架，其中四个与假单胞菌菌株的萘双氧酶（NDO）的组分具有高度相似性（59-78％的同源性）。在编码DNT双氧酶的基因中也鉴定了在NDO中参与辅因子结合的保守氨基酸残基。表达DNT双氧酶的大肠杆菌克隆将DNT转化为MNC，并将萘转化为(+)-顺式-(1R,2S)-二羟基-1,2-二氢萘。相反，表达NDO的大肠杆菌克隆不氧化DNT。此外，这些酶系统表现出类似的广泛底物特异性，可以氧化吲哚，吲哚并，茚烯，苯乙醚和蒽。这些结果表明，DNT双氧酶和NDO酶系统共享一个共同的祖先。
• Protein Engineering of the 4-Methyl-5-Nitrocatechol Monooxygenase from <i>Burkholderia</i> sp. Strain DNT for Enhanced Degradation of Nitroaromatics
  作者：Thammajun Leungsakul、Glenn R. Johnson、Thomas K. Wood

  DOI：10.1128/aem.02966-05

  日期：2006.6

  4-Methyl-5-nitrocatechol (4M5NC) monooxygenase (DntB) from Burkholderia sp. strain DNT catalyzes the second step of 2,4-dinitrotoluene degradation by converting 4M5NC to 2-hydroxy-5-methylquinone with the concomitant removal of the nitro group. DntB is a flavoprotein that has a very narrow substrate range. Here, error-prone PCR was used to create variant DntB M22L/L380I, which accepts the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP). At 300 μM of 4NP, the initial rate of the variant expressing M22L/L380I enzyme (39 ± 6 nmol/min/mg protein) was 10-fold higher than that of the wild-type enzyme (4 ± 2 nmol/min/mg protein). The values of k _cat / K _m of the purified wild-type DntB enzyme and purified variant M22L/L380I were 40 and 450 (s ⁻¹ M ⁻¹ ), respectively, which corroborates that the variant M22L/L380I enzyme has 11-fold-higher efficiency than the wild-type enzyme for 4NP degradation. In addition, the variant M22L/L380I enzyme has fourfold-higher activity toward 3M4NP; at 300 μM, the initial nitrite release rate of M22L/L380I enzyme was 17 ± 4 nmol/min/mg protein, while that of the wild-type enzyme was 4.4 ± 0.7 nmol/min/mg protein. Saturation mutagenesis was also used to further investigate the role of the individual amino acid residues at positions M22, L380, and M22/L380 simultaneously. Mutagenesis at the individual positions M22L and L380I did not show appreciable enhancement in 4NP activity, which suggested that these two sites should be mutated together; simultaneous saturation mutagenesis led to the identification of the variant M22S/L380V, with 20% enhanced degradation of 4NP compared to the variant M22L/L380I. This is the first report of protein engineering for nitrite removal by a flavoprotein.

  摘要 4-甲基-5-硝基邻苯二酚（4M5NC）单加氧酶（DntB）来自于 菌株 DNT 菌株 DNT 中的 4-甲基-5-硝基邻苯二酚（4M5NC）单加氧酶（DntB）催化 2,4-二硝基甲苯降解的第二步，将 4M5NC 转化为 2-羟基-5-甲基苯醌，同时去除硝基。DntB 是一种黄素蛋白，其底物范围很窄。在这里，我们利用易错 PCR 技术创建了变体 DntB M22L/L380I，它可以接受 4-硝基苯酚（4NP）和 3-甲基-4-硝基苯酚（3M4NP）这两种新底物。在 4NP 浓度为 300 μM 时，表达 M22L/L380I 的变体酶的初始速率（39 ± 6 nmol/min/mg）是野生型酶（4 ± 2 nmol/min/mg）的 10 倍。其值是野生型酶（4 ± 2 nmol/min/mg）的 10 倍。 k cat / K m 分别为40和450（s -1 M -1 )，这证实变体 M22L/L380I 酶降解 4NP 的效率是野生型酶的 11 倍。此外，变体 M22L/L380I 酶对 3M4NP 的活性比野生型高 4 倍；在 300 μM 的条件下，M22L/L380I 酶的初始亚硝酸盐释放率为 17 ± 4 nmol/min/mg，而野生型酶为 4.4 ± 0.7 nmol/min/mg。为了进一步研究 M22、L380 和 M22/L380 三个位置的单个氨基酸残基的作用，还同时使用了饱和诱变。单个位置 M22L 和 L380I 的突变没有显示出明显的 4NP 活性增强，这表明这两个位点应该一起突变；同时进行饱和突变后，发现了变体 M22S/L380V，与变体 M22L/L380I 相比，4NP 的降解增强了 20%。这是首次报道黄蛋白去除亚硝酸盐的蛋白质工程。
• Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT
  作者：B E Haigler、W C Suen、J C Spain

  DOI：10.1128/jb.178.20.6019-6024.1996

  日期：1996.10

  4-Methyl-5-nitrocatechol (MNC) is an intermediate in the degradation of 2,4-dinitrotoluene by Burkholderia sp. strain DNT. In the presence of NADPH and oxygen, MNC monooxygenase catalyzes the removal of the nitro group from MNC to form 2-hydroxy-5-methylquinone. The gene (dntB) encoding MNC monooxygenase has been previously cloned and characterized. In order to examine the properties of MNC monooxygenase and to compare it with other enzymes, we sequenced the gene encoding the MNC monooxygenase and purified the enzyme from strain DNT. dntB was localized within a 2.2-kb ApaI DNA fragment. Sequence analysis of this fragment revealed an open reading frame of 1,644 bp with an N-terminal amino acid sequence identical to that of purified MNC monooxygenase from strain DNT. Comparison of the derived amino acid sequences with those of other genes showed that DntB contains the highly conserved ADP and flavin adenine dinucleotide (FAD) binding motifs characteristic of flavoprotein hydroxylases. MNC monooxygenase was purified to homogeneity from strain DNT by anion exchange and gel filtration chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a single protein with a molecular weight of 60,200, which is consistent with the size determined from the gene sequence. The native molecular weight determined by gel filtration was 65,000, which indicates that the native enzyme is a monomer. It used either NADH or NADPH as electron donors, and NADPH was the preferred cofactor. The purified enzyme contained 1 mol of FAD per mol of protein, which is also consistent with the detection of an FAD binding motif in the amino acid sequence of DntB. MNC monooxygenase has a narrow substrate specificity. MNC and 4-nitrocatechol are good substrates whereas 3-methyl-4-nitrophenol, 3-methyl-4-nitrocatechol, 4-nitrophenol, 3-nitrophenol, and 4-chlorocatechol were not. These studies suggest that MNC monooxygenase is a flavoprotein that shares some properties with previously studied nitrophenol oxygenases.

  4-甲基-5-硝基邻苯二酚（MNC）是Burkholderia sp.菌株DNT分解2,4-二硝基甲苯的中间体。在NADPH和氧的存在下，MNC单加氧酶催化去除MNC中的硝基，形成2-羟基-5-甲基喹啉醌。编码MNC单加氧酶的基因（dntB）已被先前克隆和表征。为了研究MNC单加氧酶的性质并将其与其他酶进行比较，我们测序了编码MNC单加氧酶的基因并从菌株DNT中纯化了酶。dntB位于一个2.2 kb的ApaI DNA片段内。对该片段的序列分析揭示了一个开放阅读框，长度为1,644 bp，其N端氨基酸序列与从菌株DNT纯化的MNC单加氧酶相同。将推导的氨基酸序列与其他基因的序列进行比较，发现DntB包含高度保守的ADP和黄素腺嘌呤二核苷酸（FAD）结合基序，这是黄素蛋白羟化酶的特征。通过阴离子交换和凝胶过滤色谱法从菌株DNT中纯化了MNC单加氧酶至纯度。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示出一个分子量为60,200的单一蛋白质，与基因序列确定的大小一致。通过凝胶过滤法确定的天然分子量为65,000，表明天然酶是单体。它使用NADH或NADPH作为电子受体，其中NADPH是首选辅因子。纯化的酶含有每摩尔蛋白质1摩尔FAD，这也与在DntB的氨基酸序列中检测到FAD结合基序一致。MNC单加氧酶具有狭窄的底物特异性。MNC和4-硝基邻苯二酚是良好的底物，而3-甲基-4-硝基苯酚、3-甲基-4-硝基邻苯二酚、4-硝基苯酚、3-硝基苯酚和4-氯邻苯二酚则不是。这些研究表明，MNC单加氧酶是一种黄素蛋白，与先前研究的硝基苯酚加氧酶共享一些性质。
• Bis-azo colorants for use as bluing agents
  申请人：The Procter & Gamble Company

  公开号：US10041024B2

  公开（公告）日：2018-08-07

  This invention relates to bis-azo colorants for use as bluing agents, laundry care compositions comprising bis-azo colorants that may serve as bluing agents, processes for making such bluing agents and laundry care compositions and methods of using the same. The bluing agents are generally comprised of at least two components: at least one chromophore component and at least one polymeric component. These bluing agents are advantageous in providing a whitening effect to fabrics, while not building up over time and causing undesirable blue discoloration to the treated fabrics.

  本发明涉及用作发蓝剂的双偶氮着色剂、包含可用作发蓝剂的双偶氮着色剂的衣物护理组合物、制造此类发蓝剂和衣物护理组合物的工艺以及使用方法。发蓝剂一般由至少两种成分组成：至少一种发色团成分和至少一种聚合物成分。这些发蓝剂在为织物提供增白效果方面具有优势，同时不会随着时间的推移而积聚，导致处理过的织物出现不希望看到的蓝色褪色。
• Wound packing material comprising chemoeffector
  申请人：CHEMOKIND, INC.

  公开号：US11273077B2

  公开（公告）日：2022-03-15

  A wound packing material, particularly suitable for use in negative pressure wound therapy, comprising a porous material admixed with a chemoattractant. This disclosure further provides methods of manufacturing the wound packing material, and therapeutic methods of using the wound packing material.

  一种伤口填料，特别适用于负压伤口治疗，包括一种多孔材料和一种趋化吸引剂。本公开进一步提供了制造伤口填料的方法，以及使用伤口填料的治疗方法。