615-91-8

Usage

Uses

Used in Chemical Synthesis:
2-Hydroxy-5-methylquinone is used as an intermediate in the synthesis of various organic compounds and pharmaceuticals. Its unique structure allows it to participate in a range of chemical reactions, making it a valuable building block for the development of new molecules with potential applications in various industries.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 2-hydroxy-5-methylquinone is used as a key component in the development of drugs targeting specific diseases. Its chemical properties enable it to interact with biological systems, potentially leading to the creation of new therapeutic agents with improved efficacy and selectivity.
Used in Material Science:
2-Hydroxy-5-methylquinone can also be utilized in material science for the development of novel materials with unique properties. Its quinone structure and functional groups may contribute to the formation of new materials with applications in areas such as energy storage, catalysis, or sensing.

InChI:InChI=1/C7H6O3/c1-4-2-6(9)7(10)3-5(4)8/h2-3,8H,1H3

Upstream product

• 1124-09-0 1,2,4-tri-hydroxy-5-methylbenzene 
• 452-86-8 4-methyl-1,2-dihydroxybenzene 
• 147-85-3 L-proline 
• 3131-54-2 4-methylbenzo-1,2-quinone 
• 5462-27-1 2-methyl-4,5-di-acetoxyphenyl acetate 
• 553-97-9 2-Methyl-1,4-benzoquinone 

Downstream Products

• 614-13-1 2-methoxy-5-methyl-1,4-benzoquinone 
• 161678-07-5 C₁₃H₉IO₃ 
• 40815-76-7 3-allyl-2-hydroxy-1,4-naphthoquinone 
• 16635-80-6 2.6-Dihydroxy-3-methyl-benzochinon 

Relevant academic research and scientific papers

Chemical simulation of biogenesis of the 2,4,5-trihydroxyphenylalanine quinone cofactor of copper amine oxidases: Mechanistic distinctions point toward a unique role of the active site in the o-quinone water addition step

The biogenesis of the 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor from tyrosine at the active site of copper amine oxidases is believed to proceed along a pathway that includes a conjugate addition of water to the corresponding o-quinone intermediate, followed by autoxidation of the resulting benzenetriol to the hydroxyquinone cofactor. The water addition reaction has been presumed to occur not only in previous model studies reported for cofactor biogenesis starting with either catechol or o-quinone, but also for generation of the neurotoxin 6-hydroxydopamine during autoxidation of dopamine. We here report the surprising finding that water addition does not occur under solution chemistry conditions. The production of hydroxyquinone from catechol arises instead from reaction of the o-quinone with H2O2 generated during autoxidation of catechol. When starting with the o-quinone itself, production of hydroxyquinone still arises from autoxidation of the catechol, generated either by reduction of the o-quinone by its decomposition products at moderate pH, or by a novel base-mediated redox disproportionation of the o-quinone at high pH. These conclusions are supported by the behavior of independently studied o-quinone intermediates, the observed effects of added catalase, and 18O-labeling studies utilizing both [18O]H2O and [18O]O2. The failure to observe water addition to the o-quinone has broad implications for aqueous o-quinone chemistry, and suggests that in TPQ biogenesis, this hydration is being catalyzed at the enzyme active site, possibly by the bound copper.

Oxidative chemistry of the natural antioxidant hydroxytyrosol: Hydrogen peroxide-dependent hydroxylation and hydroxyquinone/o-quinone coupling pathways

Oxidation of the natural antioxidant hydroxytyrosol (1) with peroxidase/H2O2 in phosphate buffer at pH 7.4 led to the formation of two main ethyl acetate-extractable products. These could be isolated by preparative TLC after reduction and acetylation, and were identified as the tetraacetyl derivative of 2-(2,4,5-trihydroxyphenyl)ethanol (3) and the heptaacetyl derivative of the pentahydroxybiphenyl 4 by 2D NMR and MS analysis. Similar oxidation of 4-methylcatechol gave, after the same work-up, the acetylated derivatives of 1,2,4-trihydroxy-5-methylbenzene (5) and the pentahydroxybiphenyl 6. Mechanistic experiments suggested that hydrogen peroxide affects the course of the oxidation of 1 by adding to the first formed o-quinone to give a hydroxyquinone intermediate. This could bring nucleophilic attack to the o-quinone of 1 to give the dimer 4. These results disclose novel oxidative pathways of 4-alkylcatechols and provide an improved chemical basis to enquire into the mechanism of the antioxidant action of 1.

Generation of the Neurotoxin 6-Hydroxydopamine by Peroxidase/H2O2 Oxidation of Dopamine

At physiological pH values, oxidation of the neurotransmitter dopamine(DA) by the peroxidase/H2O2 system leads to, besides dopaminochrome and 5,6-dihydroxyindole resulting from oxidative cyclization of dopaminequinone (DQ), significant amounts of the neurotoxin 6-hydroxydopamine (6-OHDA) in the oxidized quinonoid form (topaminequinone, TQ).Formation of TQ was shown to depend critically on the presence of hydrogen peroxide in the reaction medium and was not observed when DA oxidation was carried out using the tyrosinase/O2 system or chemical agents such as periodate or ferricyanide.These and other data suggest that, under the conditions adopted, nucleophilic attack of the hydrogen peroxide anion on DQ leading to TQ significantly competes with the intramolecular cyclization path.In line with this mechanism, the reaction course was not affected by the presence of hydroxyl radical scavengers.Peroxidase/H2O2 oxidation of the model N-acetyldopamine (1) gave, as expected, the 2-hydroxy-1,4-benzoquinone 3 in yields up to 55percent, depending on the catecholamine/H2O2 mole ratio.Likewise, reaction of 4-methyl-1,2-benzoquinone (4) with hydrogen peroxide afforded 2-hydroxy-5-methyl-1,4-benzoquinone (5) in good yields.Collectively, these results would point to the possibility that intraneuronal formation of 6-OHDA is associated with an increased production of hydrogen peroxide under oxidative stress conditions.

REACTIONS OF 4-METHYL-o-BENZOQUINONE, GENERATED CHEMICALLY OR ENZYMATICALLY, IN THE PRESENCE OF L-PROLINE

The reactions of 4-methyl-o-benzoquinone in the presence of L- proline were studied by rapid scanning spectrophotometry.It was concluded that it was transformed into 5-methyl-4-N-prolyl-o-benzoquinone, according to the equation: 2(4-methyl-o-benzoquinone) + L-proline->4-methylcatechol + 5-methyl-4-N-prolyl-o-benzoquinone.Rate constants for the reaction of 4-methyl-o-benzoquinone with water and L-proline have been measured.Key Word Index-Tyrosinase; 4-methylcatechol; 4-methyl-o-benzoquinone; L-proline.