4018-65-9

Usage

Uses

Used in Pharmaceutical Industry:
3-Chlorocatechol is used as a reagent for synthesizing novel benzotropolones, which are known to act as Atg4B inhibitors. These inhibitors play a crucial role in blocking autophagy, a cellular process responsible for the degradation and recycling of cellular components. By inhibiting autophagy, benzotropolones can potentially be used in the development of therapeutic strategies for various diseases, including cancer and neurodegenerative disorders.
Used in Chemical Synthesis:
3-Chlorocatechol can be utilized as a building block or intermediate in the synthesis of various organic compounds, such as dyes, pharmaceuticals, and agrochemicals. The presence of the chlorine atom in the molecule allows for further functionalization and modification, enabling the creation of a wide range of derivatives with diverse applications.
Used in Research and Development:
Due to its unique chemical properties, 3-chlorocatechol can be employed in research and development for studying the effects of halogen substitution on the reactivity and stability of catechol derivatives. This can provide valuable insights into the structure-activity relationships of these compounds and contribute to the design of new molecules with improved properties and applications.

InChI:InChI=1/C6H5ClO2/c7-4-2-1-3-5(8)6(4)9/h1-3,8-9H

Upstream product

• 583-63-1 ortoquinone 
• 90282-99-8 3-chloro-1,2-dimethoxybenzene 
• 120-80-9 benzene-1,2-diol 
• 108-43-0 3-monochlorophenol 
• 603-86-1 2-chloro-6-nitrophenol 
• 7791-25-5 sulfuryl dichloride 
• 60-29-7 diethyl ether 
• 623-11-0 1-methyl-4-nitrosobenzene 
• 95-57-8 2-monochlorophenol 
• 1927-94-2 3-chlorosalicylaldehyde 
• 108-90-7 chlorobenzene 
• 86992-79-2 (1S,2S)-3-Chloro-cyclohexa-3,5-diene-1,2-diol 
• 2040-90-6 2-chloro-6-fluorophenol 
• 87-65-0 2,6-Dichlorophenol 

Downstream Products

• 77102-92-2 3-Chloro-2-methoxyphenol 
• 72403-03-3 2-methoxy-6-chlorophenol 
• 90282-99-8 3-chloro-1,2-dimethoxybenzene 
• 845830-22-0 2-chloro-6-{[(trifluoromethyl)-sulfonyl]oxy}phenyl trifluoromethanesulfonate 
• 187543-48-2 (R)-8-chloro-1,4-benzodioxan-2-ylmethyl 4-toluenesulphonate 
• 120-80-9 benzene-1,2-diol 
• 533-60-8 cyclohexanone-2-ol 
• 56961-34-3 3-Chlor-o-benzochinon 

Relevant academic research and scientific papers

Photochemical transformations of 2, 6-dichlorophenol and 2-chlorophenol with superoxide ions in the atmospheric aqueous phase

The possible photochemical transformation pathways of chlorophenols (2, 6-dichlorophenol and 2-chlorophenol) with superoxide anion radical (O2·?) were studied by steady-state irradiation and 355 nm laser flash photolysis technique. O

A new avenue to the Dakin reaction in H2O2-WERSA

We have developed a novel protocol to realize the Dakin reaction in a more greener way. In fact, by the use of H2O2-WERSA, we can oxidize aromatic arylaldehydes to phenols at room temperature. It is remarkable that the catalytic system does not require activation or any toxic ligand, additive/promoter, transition metal catalyst, base, organic solvent and so on. A range of substituted hydroxylated benzaldehydes were screened to investigate the scope of this protocol.

Selective ortho-hydroxylation-defluorination of 2-fluorophenolates with a Bis(μ-oxo)dicopper(III) species

The bis(μ-oxo)dicopper(III) species [CuIII 2(μ-O)2(m-XYLMeAN)]2+ (1) promotes the electrophilic ortho-hydroxylation-defluorination of 2-fluorophenolates to give the corresponding catechols, a reaction that is not accomplishable with a (η2:η2-O2) dicopper(II) complex. Isotopic labeling studies show that the incoming oxygen atom originates from the bis(μ-oxo) unit. Ortho-hydroxylation-defluorination occurs selectively in intramolecular competition with other ortho-substituents such as chlorine or bromine. O in, F out: [CuIII2(μ-O) 2(m-XYLMeAN)]2+ is a bis(μ-oxo)dicopper(III) species and promotes the electrophilic ortho-hydroxylation-defluorination of 2-fluorophenolates to give the corresponding catechols. Isotopic labeling shows that the incoming oxygen atom originates from the bis(μ-oxo) unit. Ortho-hydroxylation-defluorination occurs selectively in intramolecular competition with other ortho-substituents such as chlorine or bromine.

Structure, stereochemistry and synthesis of enantiopure cyclohexenone cis-diol bacterial metabolites derived from phenols

Biotransformation of 3-substituted and 2,5-disubstituted phenols, using whole cells of P. putida UV4, yielded cyclohexenone cis-diols as single enantiomers; their structures and absolute configurations have been determined by NMR and ECD spectroscopy, X-ray crystallography, and stereochemical correlation involving a four step chemoenzymatic synthesis from the corresponding cis-dihydrodiol metabolites. An active site model has been proposed, to account for the formation of enantiopure cyclohexenone cis-diols with opposite absolute configurations.

Aerobic organocatalytic oxidation of aryl aldehydes: Flavin catalyst turnover by Hantzsch's ester

The first Dakin oxidation fueled by molecular oxygen as the terminal oxidant is reported. Flavin and NAD(P)H coenzymes, from natural enzymatic redox systems, inspired the use of flavin organocatalysts and a Hantzsch ester to perform transition-metal-free, aerobic oxidations. Catechols and electron-rich phenols are achieved with as low as a 0.1 mol % catalyst loading, 1 equiv of Hantzsch ester, and O2 or air as the stoichiometric oxidant source.

A comparative study of the synthesis of 3-substituted catechols using an enzymatic and a chemoenzymatic method

A series of cis-dihydrodiol metabolites, available from the bacterial dioxygenase-catalysed oxidation of monosubstituted benzene substrates using Pseudomonas putida UV4 , have been converted to the corresponding catechols using both a heterogeneous catalyst (Pd/c) and a naphthalene cis-diol dehydrogenase enzyme present in whole cells of the recombinant strain Escherichia coli DH5α(pUC129: nar B). A comparative study of the merits of both routes to 3-substituted catechols has been carried out and the two methods have been found to be complementary. A similarity in mechanism for catechol formation under both enzymatic and chemoenzymatic conditions, involving regioselective oxidation of the hydroxyl group at C-1, has been found using deuterium labelled toluene cis-dihydrodiols. The potential, of combining a biocatalytic step (dioxygenase-catalysed cis-dihydroxylation) with a chemocatalytic step (Pd/C-catalysed dehydrogenation), into a one-pot route to catechols, from the parent substituted benzene substrates, has been realised.

One-pot synthesis of substituted catechols from the corresponding phenols

Phenols are converted to salicylaldehydes with paraformaldehyde, MgCl 2-Et3N in THF, and when subsequently treated with aqueous NaOH and H2O2 afford the corresponding catechols. The sequence is conveniently carried out as a one-pot procedure.

Biocatalytic synthesis of polycatechols from toxic aromatic compounds

A process is described in which toxic aromatic compounds are converted by toluene dioxygenase and in turn toluene cis-dihydrodiol dehydrogenase to catechols which are further polymerized by peroxidase-catalyzed oxidation producing polycatechols. Three approaches for obtaining catechols were employed: (1) addition of halogenated aromatics to P. putida F1, resulting in the accumulation of halogenated catechols; (2) inhibition of catechol 2,3-dioxygenase of P. putida F1 by known aromatic and aliphatic inhibitors; and (3) overexpression of toluene dioxygenase and toluene cis-dihydrodiol dehydrogenase genes in E. coli JM109. The process is suitable for producing novel catechols that upon oxidation may yield polymers with unique properties, presenting a tool for producing tailor-made biopolymers. Formation of 3-chlorocatechol from chlorobenzene, 3,4-dichlorocatechol from 1,2-dichlorobenzene, and catechol from benzene and their subsequent oxidation and polymerization was demonstrated. Oxidation of catechol yielded polymers with molecular weights of up to 4000 Daltons. Their apparently high water solubility eliminates the need for water-miscible solvents. In aqueous solution oxidation of catechols was rapid, yet the presence of 20%, 30%, and 40% ethanol, resulted in a rate decrease of 31%, 95%, and 93%, respectively. The advantage is that significantly less peroxidase is required for performing the reactions if miscible solvents are not employed. Furthermore, water-soluble polymers may be desirable for many applications.

Medium-scale preparation of useful metabolites of aromatic compounds via whole-cell fermentation with recombinant organisms

The whole-cell fermentation of aromatic coumpounds with Escherichia coli JM109 (pDTG601) on a medium scale (10-15L) produces enantiopure cyclohexadienediols. A detailed procedure for the fermentation is described, and yields for several metabolites are provided. A similar procedure using E. coli JM109 (pDTG602) affords catechols. The dienediols are useful for asymmetric synthesis, and several important targets originating from these metabolites are tabulated.

Comparison of Substituted 2-Nitrophenol Degradation by Enzyme Extracts and Intact Cells

The first catabolic pathway enzyme, nitrophenol oxygenase, transforms o-nitrophenol (ONP) to catechol. Thirteen of 16 substituted nitrophenols tested were actively transformed by both enzyme preparations and intact cells yielding a wide range of Km (Ks) and Vmax. Individual chemicals in binary mixtures demonstrated competitive inhibition. Chemical and physical characteristics (electron withdrawal, size, and position of substitution on the 2-nitrophenol ring) affected degradation kinetics. The strongest correlation were between Km or Vmax values and electron withdrawal, though there was also evidence for effects relating to position and size of substitution on the aromatic ring. Kinetic parameters determined for enzyme preparations did not correlate to those determined for intact cells. Though enzyme reactivity ultimately determined whether a given chemical would be transformed, the transformation by intact cells was apparently affected by factors other than those directly impacting the initial catabolic enzyme.