• Microbiology and Biotechnology Letters
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• v.17 no.3
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• pp.224-230
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• 1989

For the production of catechol from benzene, bacteria capable of assimilating benzene as a sole carbon and energy source were isolated from soils. Among them, newly isolated strain, KY-114 hay-ing the best ability of producing catechol from benzene was selected and a mutant Pseudomonas sp. HW-103 was developed from Pseudomonas sp. KY-114 by using mutagenesis induced by N-methyl - N'- nitro - N -nitrobo guanidine. The catechol reduction from benzone by Pseudomonas sp. HW-103 was investigated under various conditions. The highest catechol concentration (0.61 g/$\ell$) was obtained in the growth medium (pH 6.5) containing 1% sodium citrate, 0.75% (NH$_4$)$_2$SO$_4$, 0.15% benzene and other minerals at 3$0^{\circ}C$ after incubating of 15hrs. In the catechol production through the reaction with resting rolls, 2.5 g/1 of catechol was produced from 4 g/$\ell$ of benzene after incubation of 10 hrs under the optium conditions, which correponds to 45% of theoretical catechol yield.

• Biomedical Science Letters
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• v.25 no.1
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• pp.1-6
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• 2019

The hydroxylation of estradiol results in the formation of catechol estrogens such as 2-hydroxyestradiol ($2-OHE_2$) and 4-hydroxyestradiol ($4-OHE_2$). These catechol estrogens are further oxidized to quinone metabolites by peroxidases or cytochrome P450 (CYP450) enzymes. Catechol estrogens contribute to hormone-induced carcinogenesis by generating DNA adducts or reactive oxygen species (ROS). Interestingly, many of the natural products found in living organisms have been reported to show protective effects against carcinogenesis induced by catechol estrogens. Although some compounds have been reported to increase the activity of catechol estrogens via oxidation to quinone metabolites, many natural products decreased the activity of catechol estrogens by inhibiting DNA adduct formation, ROS production, or oxidative cell damage. Here we focus specifically on the chemopreventive effects of these natural compounds against carcinogenesis induced by catechol estrogens.

• Archives of Pharmacal Research
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• v.15 no.1
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• pp.48-51
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• 1992

Achromobacter xylosoxidans KF701 and Pseudomonas putida (NAH7) were significantly different in degradative capability of aromatic compounds including benzoates, biphenyls, and naphthalene. However, both of the bacterial strains can grown on catechol as the sole carbon and energy source. Catechol 2, 3-dioxygenase gene for naphthalene oxidation or biphenyl oxidation was cloned into Escherichia coli HB 701. A E. coli HB 101 clone containing catechol 2, 3-dioxygenase gene from P. putida (NAH7) contains a recombinant plasmid with 3.60kb pBR322 and 6-kb insert DNA. Another E. coli HB101 clone containing catechol 2, 3-dioxygenase gene from A. xylosoxidans KF 701 has a recombinant plasmid with 4.4kb pBR322 and 10-kb insert DNA. Physical maps of the recombinant plasmids were constructed, and catechol 2, 3-dioxygenase gene in the recombinant plasmide was further localized and subcloned int M13. The cloned-catechol 2, 3-dioxygenase game products were identified as yellow bands on nondenaturaing polyacrylamide gel after electrophoresis followed by activity staining with catechol solution.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.54 no.5
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• pp.644-651
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• 2021

Viral hemorrhagic septicemia virus (VHSV) is a fish pathogen responsible for causing enormous economic loss to the aquaculture industry not only in Korea but worldwide. Thus, it is necessary to identify natural compounds that can be used to control the spread of VHSV. In this study, the anti-VHSV activities of five catechol derivatives, i.e., catechol, pyrogallol, 3-methyl catechol, veratrole, and 3-methyl veratrole-extracted from green tea-were assessed. The antiviral activities of these derivatives were found to be dependent on their structure, i.e., the hydroxyl or methoxyl group and their substituent groups-on the benzene ring. Catechol, pyrogallol, and 3-methyl catechol exhibited relatively high 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities than veratrole, and 3-methyl veratrole. Moreover, 3-methyl catechol harboring a methyl substituent group increased the viability of the virus-infected cells and resulted in a 2.86 log reduction in the gene copies of VHSV N (per mL) in real-time PCR analysis. In conclusion, the catechol derivatives harboring hydroxyl groups in their benzene ring exhibited higher antioxidant activities than those harboring the methoxyl groups. However, catechol derivatives with a methyl group at the 3'-position of the benzene ring exhibited higher antiviral activity than those harboring a hydroxyl group. To our knowledge, this is the first study to evaluate the relationship between the structure and the anti-VHSV activity of catechol derivatives.

• Journal of Microbiology and Biotechnology
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• v.16 no.5
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• pp.778-785
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• 2006

Catechol 1,2-dioxygenase was purified from cells of R. rhodochrous N75 grown at the expense of benzoate and p-toluate as the sole sources of carbon. A single catechol 1,2-dioxygenase was found to be induced with either growth substrate. The enzyme has an estimated $M_r$ of 71,000 consisting of two identical subunits. Catechol 1,2-dioxygenase from R. rhodochrous N75 exhibits some unusual properties including: broad substrate specificity, extradiol cleavage activity with 4-methylcatechol and low $K_m$ values for halocatechols, suggesting that this enzyme is distinct from other known catechol and chlorocatechol 1,2-dioxygenases.

• Korean Journal of Microbiology
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• v.35 no.2
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• pp.139-145
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• 1999

Aromatic hydrocarbons which are not easily degraded by microorganisms can be accumulated in the conlaminated environment for a long lime, producing toxic effects on wild lives and humans. However, the sublethal concentrations of the chemicals induce the synthesis of stress-shock proteins in the cells and increase the adaptability of the organisms to the environmental stresses. In this study, therefore, the cells of Psezido~nonus sp. DJ- 12 treated with catechol at various concentrations were inveshgated for their survival, biodegtadability of catechol, production of stress-shock proteins, and cytological changes. The organisms were capable of degrading catechol at the range of 0.5 to 1.0 mM concentration wilhin 6 hours incubation, but they were killed by $10^2$-10$^3$ celllinl at 3 mM or higel- concentration without any catechol degradation. These cells treated with catechol begm lo produce DnaK and GroEL at 1 mM and 0.5 mM. respectively. Pseudumonas sp. DJ-12 treated with 10 mM catechol for I hour exhihiled some punctuated pores on the cell wall and contortion of the rod shape. The cells treated with he sublethal concentration of catechol showed the increased tolerance for suvival when exposed to the lethal concentration, and such tolerant effects were functioned crossly among benzoate, 4-chlorobenzoate, 'and catechol.

• Korean Journal of Microbiology
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• v.29 no.3
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• pp.155-159
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• 1991

Four strains of Pseudomonas putida (NAH), Pseudomonas sp.(TOL), Achromobacter xylosoxidans, and Alcaligenes sp. were compared with their degradative capability of aromatic compounds. All of the bacterial strains were utilized catechol as a sole carbon source for growth, but signigicantly different in degradative properties for 5 other aromatic compounds. Catechol 2, 3-dioxygenase gene from P. putida (NAH) has been cloned and expressed in E. coli. The DNA clone designated pCNU101 contains NAH-derived 6 Kb insert and its physical map was characterized. A subclone (pCNU106) for the catechol dioxygenase gene in pCNU101 contained 2.0kb-DNA insery fragmented by HpaI and ClaI.

• Analytical Science and Technology
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• v.18 no.5
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• pp.369-375
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• 2005

The differential pulse anode stripping voltammograms of some rare earth elements and their complexes with catechol have been investigated in various pH and electrolytes. In a 0.1 M LiCl and pH 5.3 solution, $Euv^{3+}$ and $Pr^{3+}$ showed a single oxidation peak at -0.2 V and the oxidation currents were linearly increased with the concentration of those ions. $Tm^{3+}$, $Tb^{3+}$, $Yb^{3+}$ and $Sm^{3+}$ showed two oxidation peaks at -0.5 V and -0.2 V and the oxidation currents at -0.5 V were increased with the concentration increase of those ions. The linear range of those calibration curves was in 1 ppm-10 ppm. In the case of voltammograms of catechol complexes of rare earth elements, $Tb^{3+}$-catechol and $Eu^{3+}$-catechol complex showed a single oxidation peak at -0.95 V and -0.65V, respectively and $Sm^{3+}$-catechol, $Pr^{3+}$-catechol, $Tm^{3+}$-catechol and $Yb^{3+}$-catechol complexes showed two oxidation peaks. The linear range of the calibration curves of those complex was 0.1 ppm~1.0 ppm.

• Biomedical Science Letters
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• v.24 no.3
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• pp.143-149
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• 2018

Excessive exposure to estrogens is the most important risk factor for the development of hormone-sensitive cancers, especially breast cancer. Estrogen stimulates the expression of genes and proteins involved in cell proliferation by binding to estrogen receptor (ER). Another possible mechanism of ER-independent carcinogenicity of estrogens is based on the hydroxylation of estradiol resulting in the formation of catechol estrogens. Catechol estrogen 4-hydroxyestradiol ($4-OHE_2$) is further oxidized to catechol estrogen-3,4-quinones, the major carcinogenic metabolites of estrogens. Evidence increasingly supports the critical role of $4-OHE_2$ in hormonal carcinogenesis via DNA adduct formation or production of reactive oxygen species, which finally contribute to the transformation of normal mammary epithelial cells and the enhanced growth of breast cancer cells. It is also reported that the level of $4-OHE_2$ or its quinones is highly up-regulated in urine or tissues of breast cancer patients. Thus, we highlight the oncogenic roles of $4-OHE_2$ in catechol estrogen-induced breast carcinogenesis.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.112-114
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• 1998

For enhancement of cis,cis-muconate productivity from benzoate, catechol 1,2-dioxygenase (C12O) which catalyzes the rate-limiting step (catechol conversion to cis,cis-muconate) was cloned and expressed in recombinant Pseudomonas putida BCM114. At higher benzoate concentrations (more than 15 mM), cis,cis-muconate productivity gradually decreased and unconverted catechol was accumulated up to 10 mM in the cae of wild-type P. putida BM014, whereas cis,cis-muconate productivity continuously increased and catechol was completely transformed to cis,cis-muconate for P. putida BCM114. Specific C12O activity of P. putida BCM114 was about three times higher than that of P. putida BM014, and productivity was enhanced more than two times.