3333-25-3

Usage

Uses

Used in Organic Synthesis:
1,3-Dibromo-2,5-dihydroxybenzene is used as a building block in organic synthesis for the preparation of various other compounds. Its unique structure allows for further chemical reactions and modifications, making it a valuable intermediate in the synthesis of complex organic molecules.
Used in Pharmaceutical Production:
1,3-Dibromo-2,5-dihydroxybenzene is used as a reagent in the production of pharmaceuticals. Its chemical properties enable it to be incorporated into the synthesis of various drug molecules, contributing to the development of new therapeutic agents.
Used in Agrochemical Production:
1,3-Dibromo-2,5-dihydroxybenzene is also utilized in the production of agrochemicals. Its potential applications in this industry include the development of pesticides, herbicides, and other agricultural chemicals that can help improve crop yields and protect plants from pests and diseases.
Used in Biological and Medicinal Research:
1,3-Dibromo-2,5-dihydroxybenzene has been studied for its potential biological and medicinal properties. It has shown promise as an anti-inflammatory and antioxidant agent, which could be beneficial in the treatment of various diseases and conditions. However, further research is needed to fully understand its therapeutic potential and safety.
Used in Chemical Research:
1,3-Dibromo-2,5-dihydroxybenzene is also used in chemical research to study its properties and explore its potential applications in various fields. Researchers are interested in understanding its reactivity, stability, and interactions with other molecules, which can provide valuable insights for the development of new materials and technologies.

InChI:InChI=1/C6H4Br2O2/c7-4-1-3(9)2-5(8)6(4)10/h1-2,9-10H

Upstream product

• 3958-82-5 2-bromo-1,4-benzoquinone 
• 608-33-3 2,6-dibromophenol 
• 19643-45-9 2,6-dibromo-1,4-benzoquinone 
• 123-31-9 hydroquinone 
• 2973-77-5 3,5-dibromo-4-hydroxybenzaldehyde 
• 7722-84-1 dihydrogen peroxide 
• 2423-74-7 1-acetoxy-2,6-dibromo-4-methoxyphenol 
• 150-76-5 4-methoxy-phenol 
• 106-41-2 4-bromo-phenol 
• 20244-61-5 2,4,4,6-Tetrabromo-2,5-cyclohexadien-1-one 

Downstream Products

• 19643-45-9 2,6-dibromo-1,4-benzoquinone 
• 13670-73-0 3,5-dibromo-4-methoxyphenol 
• 74076-59-8 2,6-dibromo-1,4-dimethoxybenzene 
• 2423-74-7 1-acetoxy-2,6-dibromo-4-methoxyphenol 
• 533884-35-4 1,3-dibromo-2,5-bis(methoxymethoxy)benzene 
• 1597486-70-8 C₄₃H₄₅N₅O₁₀Pd 
• 1597432-45-5 C₄₃H₄₇N₅O₁₀ 
• 100940-12-3 2,5-dimethoxy-3-bromobenzoic acid 
• 172334-49-5 (E)-2-bromo-4-oxohex-2-enedioic acid 
• 861785-99-1 1,3-dibromo-2,5-dimethoxy-4,6-dinitro-benzene 
• 2237-20-9 2,6-Dibrom-hydrochinon-dibenzylaether 
• 13670-72-9 3,5-Dibrom-4-benzyloxy-phenol 

Relevant academic research and scientific papers

Peptide-Catalyzed Fragment Couplings that Form Axially Chiral Non-C2-Symmetric Biaryls

We have demonstrated that small, modular, tetrameric peptides featuring the Lewis-basic residue β-dimethylaminoalanine (Dmaa) are capable of atroposelectively coupling naphthols and ester-bearing quinones to yield non-C2-symmetric BINOL-type scaffolds with good yields and enantioselectivity. The study culminates in the asymmetric synthesis of backbone-substituted scaffolds similar to 3,3′-disubstituted BINOLs, such as (R)-TRIP, with good (94:6 e.r.) to excellent (>99.9:0.1 e.r.) enantioselectivity after recrystallization, and a diastereoselective net arylation of the minimally modified nonsteroidal anti-inflammatory drug (NSAID) naproxen.

Novel bioactivation pathway of benzbromarone mediated by cytochrome P450

Benzbromarone (BBR) is a hepatotoxic drug, but the detailed mechanism of its toxicity remains unknown. We identified 2,6-dibromohydroquinone (DBH) and mono-debrominated catechol (2-ethyl-3-(3-bromo-4,5-dihydroxybenzoyl) benzofuran; CAT) as novel metabolites of BBR in rat and human liver microsomal systems by comparison with chemically synthesized authentic compounds, and we also elucidated that DBH is formed by cytochrome P450 2C9 and that CAT is formed mainly by CYP1A1, 2D6, 2E1, and 3A4. Furthermore, CAT, DBH, and the oxidized form of DBH are highly cytotoxic in HepG2 compared with BBR. Taken together, our data demonstrate that DBH, a novel reactive metabolite, may be relevant to BBR-induced hepatotoxicity.

Substrate specificity of Sphingobium chlorophenolicum 2,6- dichlorohydroquinone 1,2-dioxygenase

PcpA is an aromatic ring-cleaving dioxygenase that is homologous to the well-characterized Fe(II)-dependent catechol extradiol dioxygenases. This enzyme catalyzes the oxidative cleavage of 2,6-dichlorohydroquinone in the catabolism of pentachlorophenol by Sphingobium chlorophenolicum ATCC 39723. 1H NMR and steady-state kinetics were used to determine the regiospecificity of ring cleavage and the substrate specificity of the enzyme. PcpA exhibits a high degree of substrate specificity for 2,6-disubstituted hydroquinones, with halogens greatly preferred at those positions. Notably, the kcat app/KmAapp of 2,6-dichlorohydroquinone is ～40-fold higher than that of 2,6-dimethylhydroquinone. The asymmetric substrate 2-chloro-6-methylhydroquinone yields a mixture of 1,2- and 1,6-cleavage products. These two modes of cleavage have different K mO2app values (21 and 260 μM, respectively), consistent with a mechanism in which the substrate binds in two catalytically productive orientations. In contrast, monosubstituted hydroquinones show a limited amount of ring cleavage but rapidly inactivate the enzyme in an O2-dependent fashion, suggesting that oxidation of the Fe(II) may be the cause. Potent inhibitors of PcpA include ortho-disubstituted phenols and 3-bromocatechol. 2,6-Dibromophenol is the strongest competitive inhibitor, consistent with PcpA's substrate specificity. Several factors that could yield this specificity for halogen substituents are discussed. Interestingly, 3-bromocatechol also inactivates the enzyme, while 2,6-dihalophenols do not, indicating a requirement for two hydroxyl groups for ring cleavage and for enzyme inactivation. These results provide mechanistic insights into the hydroquinone dioxygenases.

Benzopyrans as selective estrogen receptor β agonists (SERBAs). Part 4: Functionalization of the benzopyran A-ring

Benzopyrans are selective estrogen receptor (ER) β agonists (SERBAs), which bind the ER receptor subtypes α and β in opposite orientations. We have used structure based drug design to show that this unique phenomena can be exploited via substitution at the 8-position of the benzopyran A-ring to disrupt binding to ERα, thus improving ERβ subtype selectivity. X-ray cocrystal structures with ERα and ERβ are supportive of this approach to improve selectivity in this structural class.

SUBSTITUTED BENZOPYRANS AS SELECTIVE ESTROGEN RECEPTOR-BETA AGONISTS

The present invention relates to substituted benzopyran derivatives, stereoisomers, and pharmaceutical acceptable salts thereof and processes for the preparation of the same. The compounds of the present invention are useful as Estrogen Receptor ? agonists. Such agonists are useful for the treating Estrogen Receptor ? mediated diseases such as prostate cancer or BPH.