1,2,4-Trihydroxybenzene
(Synonyms: 1,2,4-三羟基苯) 目录号 : GC61898
1,2,4-Trihydroxybenzene (Hydroxyhydroquinone) 是咖啡豆烘焙的副产物，可增加大鼠胸腺淋巴细胞中 Ca2+ 浓度。
Cas No.:533-73-3
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
1,2,4-Trihydroxybenzene (Hydroxyhydroquinone), a by-product of coffee bean roasting, increases intracellular Ca2+ concentration in rat thymic lymphocytes[1].
References:
[1]. Risa Kamae, et al. Hydroxyhydroquinone, a by-product of coffee bean roasting, increases intracellular Ca2+ concentration in rat thymic lymphocytes. Food Chem Toxicol. 2017 Apr;102:39-45.
| Cas No. | 533-73-3 | SDF | |
| 别名 | 1,2,4-三羟基苯 | ||
| Canonical SMILES | OC1=CC=C(O)C=C1O | ||
| 分子式 | C6H6O3 | 分子量 | 126.11 |
| 溶解度 | 储存条件 | Store at -20°C | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 7.9296 mL | 39.6479 mL | 79.2959 mL |
| 5 mM | 1.5859 mL | 7.9296 mL | 15.8592 mL |
| 10 mM | 0.793 mL | 3.9648 mL | 7.9296 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Characterization of two 1,2,4-Trihydroxybenzene 1,2-dioxygenases from Phanerochaete chrysosporium
Appl Microbiol Biotechnol 2022 Jun;106(12):4499-4509.PMID:35687156DOI:10.1007/s00253-022-12007-9.
Lignin is the most abundant aromatic compound in nature, and it plays an important role in the carbon cycle. White-rot fungi are microbes that are capable of efficiently degrading lignin. Enzymes from these fungi possess exceptional oxidative potential and have gained increasing importance for improving bioprocesses, such as the degradation of organic pollutants. The aim of this study was to identify the enzymes involved in the ring cleavage of the lignin-derived aromatic 1,2,4-Trihydroxybenzene (THB) in Phanerochaete chrysosporium, a lignin-degrading basidiomycete. Two intradiol dioxygenases (IDDs), PcIDD1 and PcIDD2, were identified and produced as recombinant proteins in Escherichia coli. In the presence of O2, PcIDD1 and PcIDD2 acted on eight and two THB derivatives, respectively, as substrates. PcIDD1 and PcIDD2 catalyze the ring cleavage of lignin-derived fragments, such as 6-methoxy-1,2,4-trihydroxybenzene (6-MeOTHB) and 3-methoxy-1,2-catechol. The current study also revealed that syringic acid (SA) was converted to 5-hydroxyvanillic acid, 2,6-dimethoxyhydroquinone, and 6-MeOTHB by fungal cells, suggesting that PcIDD1 and PcIDD2 may be involved in aromatic ring fission of 6-MeOTHB for SA degradation. This is the first study to show 6-MeOTHB dioxygenase activity of an IDD superfamily member. These findings highlight the unique and broad substrate spectra of PcIDDs, rendering it an attractive candidate for biotechnological application. KEY POINTS: • Novel intradiol dioxygenases (IDD) in lignin degradation were characterized. • PcIDDs acted on lignin-derived fragments and catechol derivatives. • Dioxygenase activity on 6-MeOTHB was identified in IDD superfamily enzymes.
Preparation of Gold Nanorods Using 1,2,4-Trihydroxybenzene as a Reducing Agent
J Nanosci Nanotechnol 2015 Aug;15(8):6230-5.PMID:26369231DOI:10.1166/jnn.2015.10626.
We report an improved method for synthesizing gold nanorods (GNRs) by using 1,2,4-Trihydroxybenzene as a reducing agent. The method allows a rich array of monodispersed GNRs with longitudinal surface plasmon resonance (LSPR) tunable from 698 to 913 nm to be generated. A large range of diameter distribution of GNRs from 9.3 to 32.2 nm with exceptional monodispersity can be well prepared by this method. These findings indicate that this method has greater performance in controlling the morphology of GNRs than that of traditional approaches with ascorbic acid as a reductant.
Purification and characterization of a 1,2,4-Trihydroxybenzene 1,2-dioxygenase from the basidiomycete Phanerochaete chrysosporium
J Bacteriol 1994 Aug;176(16):4838-44.PMID:8050996DOI:10.1128/jb.176.16.4838-4844.1994.
1,2,4-Trihydroxybenzene (THB) is an intermediate in the Phanerochaete chrysosporium degradation of vanillate and aromatic pollutants. A P. chrysosporium intracellular enzyme able to oxidatively cleave the aromatic ring of THB was purified by ammonium sulfate precipitation, hydrophobic and ion-exchange chromatographies, and native gel electrophoresis. The native protein has a molecular mass of 90 kDa and a subunit mass of 45 kDa. The enzyme catalyzes an intradiol cleavage of the substrate aromatic ring to produce maleylacetate. 18O2 incorporation studies demonstrate that molecular oxygen is a cosubstrate in the reaction. The enzyme exhibits high substrate specificity for THB; however, catechol cleavage occurs at approximately 20% of the optimal rate. THB dioxygenase catalyzes a key step in the degradation pathway of vanillate, an intermediate in lignin degradation. Maleylacetate, the product of THB cleavage, is reduced to beta-ketoadipate by an NADPH-requiring enzyme present in partially purified extracts.
Hydroxyhydroquinone reductase, the initial enzyme involved in the degradation of hydroxyhydroquinone (1,2,4-Trihydroxybenzene) by Desulfovibrio inopinatus
Arch Microbiol 2000 Mar;173(3):206-12.PMID:10763753DOI:10.1007/s002039900130.
The recently isolated sulfate reducer Desulfovibrio inopinatus oxidizes hydroxyhydroquinone (1,2,4trihydroxybenzene; HHQ) to 2 mol acetate and 2 mol CO2 (mol substrate)-1, with stoichiometric reduction of sulfate to sulfide. None of the key enzymes of fermentative HHQ degradation, i.e. HHQ-1,2,3,5-tetrahydroxybenzene transhydroxylase or phloroglucinol reductase, were detected in cell-free extracts of D. inopinatus, indicating that this bacterium uses a different pathway for anaerobic HHQ degradation. HHQ was reduced with NADH in cell-free extracts to a nonaromatic compound, which was identified as dihydrohydroxyhydroquinone by its retention time in HPLC separation and by HPLC-mass spectrometry. The compound was identical with the product of chemical reduction of HHQ with sodium borohydride. Dihydrohydroxyhydroquinone was converted stoichiometrically to acetate and to an unknown coproduct. HHQ reduction was an enzymatic activity which was present in the cell-free extract at 0.25-0.30 U (mg protein)-1, with a pH optimum at 7.5. The enzyme was sensitive to sodium chloride, potassium chloride, EDTA, and o-phenanthroline, and exhibited little sensitivity towards sulfhydryl group reagents, such as copper chloride or p-chloromercuribenzoate.
Fe-superoxide dismutase and 2-hydroxy-1,4-benzoquinone reductase preclude the auto-oxidation step in 4-aminophenol metabolism by Burkholderia sp. strain AK-5
Biodegradation 2011 Feb;22(1):1-11.PMID:20480210DOI:10.1007/s10532-010-9369-5.
Burkholderia sp. strain AK-5 converts 4-aminophenol to maleylacetic acid via 1,2,4-Trihydroxybenzene, which is unstable in vitro and non-enzymatically auto-oxidized to 2-hydroxy-1,4-benzoquinone. Crude extract of strain AK-5 retarded the auto-oxidation and reduced the substrate analogue, 2,6-dimethoxy-1,4-benzoquinone, in the presence of NADH. The two enzymes responsible were purified to homogeneity. The deduced amino acid sequence of the enzyme that inhibited the auto-oxidation showed a high level of identity to sequences of iron-containing superoxide dismutases (Fe-SODs) and contained a conserved metal-ion-binding site; the purified enzyme showed superoxide dismutase activity and contained 1 mol of Fe per mol of enzyme, identifying it as Fe-SOD. Among three type SODs tested, Fe-SOD purified here inhibited the auto-oxidation most efficiently. The other purified enzyme showed a broad substrate specificity toward benzoquinones, including 2-hydroxy-1,4-benzoquinone, converting them to the corresponding 1,4-benzenediols; the enzyme was identified as 2-hydroxy-1,4-benzoquinone reductase. The deduced amino acid sequence did not show a high level of identity to that of benzoquinone reductases from bacteria and fungi that degrade chlorinated phenols or nitrophenols. The indirect role of Fe-SOD in 1,2,4-Trihydroxybenzene metabolism is probably to scavenge and detoxify reactive species that promote the auto-oxidation of 1,2,4-Trihydroxybenzene in vivo. The direct role of benzoquinone reductase would be to convert the auto-oxidation product back to 1,2,4-Trihydroxybenzene. These two enzymes together with 1,2,4-Trihydroxybenzene 1,2-dioxygenase convert 1,2,4-Trihydroxybenzene to maleylacetic acid.