1119-72-8Relevant articles and documents
Transformation of Aromatic Compounds under the Action of the Basidiomycetes Phanerochaete sanguinea and Coriolus villosus
Medvedeva, S. A.,Volchatova, I. V.,Babkin, V. A.,Antipova, I. A.,Kanitskaya, L. V.,et al.
, p. 754 - 763 (1994)
The pathways of the transformation of some aromatic compounds by the basidiomycetes Phanerochaete sanguinea and Coriolus villosus have been studied.It has been shown that the degradation of these compounds has an oxidative nature and depends on the type of substituents in the benzene ring and the propane chain.A differencew has been found in the mechanisms of the reactions of the two fungi that is a consequence of the different compositions of their enzyme complexes.
Catechol 2,3-dioxygenase from Pseudomonas sp. strain ND6: Gene sequence and enzyme characterization
Jiang, Yun,Yang, Xianglong,Liu, Bin,Zhao, Huabing,Cheng, Qiuxiang,Cai, Baoli
, p. 1798 - 1800 (2004)
The catechol 2,3-dioxygenase (C23O) gene in naphthalene catabolic plasmid pND6-1 of Pseudomonas sp. ND6 was cloned and sequenced. The C23O gene was consisted of 924 nucleotides and encoded a polypeptide of molecular weight 36 kDa containing 307 amino acid residues. The C23O of Pseudomonas sp. ND6 exhibited 93% and 89% identities in amino acid sequence with C23Os encoded by naphthalene catabolic plasmid NAH7 from Pseudomonas putida G7 and the chromosome of Pseudomonas stutzeri AN10 respectively. The Pseudomonas sp. ND6 C23O gene was overexpressed in Escherichia coli DH 5α using the lac promoter of pUC18, and its gene product was purified by DEAE-Sephacel and Phenyl-Sepharose CL-4B chromatography. The enzymology experiments indicated that the specific activity and thermostability of C23O from Pseudomonas sp. ND6 were better than those of C23O from Pseudomonas putida G7.
KINETICS AND MECHANISM OF THE REACTION OF OZONE WITH PHENOL IN ALKALINE MEDIA
Konstantinova, M. L.,Razumovskii, S. D.,Zaikov, G. E.
, p. 266 - 270 (1991)
The kinetics of the reaction of O3 with PhOH in alkaline medium has been studied.The rate of oxidation of phenol by ozone is directly proportional to the concentrations of reactants and increases in a complex manner with increase in alkali content in aque
An isolated Candida albicans TL3 capable of degrading phenol at large concentration
Tsai, San-Chin,Tsai, Li-Duan,Li, Yaw-Kuen
, p. 2358 - 2367 (2005)
An isolated yeast strain was grown aerobically on phenol as a sole carbon source up to 24 mM; the rate of degradation of phenol at 30°C was greater than other microorganisms at the comparable phenol concentrations. This microorganism was further identified and is designated Candida albicans TL3. The catabolic activity of C. albicans TL3 for degradation of phenol was evaluated with the Ks and Vmax values of 1.7 ± 0.1 mM and 0.66 ± 0.02 μmol/min/mg of protein, respectively. With application of enzymatic, chromatographic and mass-spectrometric analyses, we confirmed that catechol and cis,cis-muconic acid were produced during the biodegradation of phenol performed by C. albicans TL3, indicating the occurrence of an ortho-fission pathway. The maximum activity of phenol hydroxylase and catechol-1,2-dioxygenase were induced when this strain grew in phenol culture media at 22 mM and 10 mM, respectively. In addition to phenol, C. albicans TL3 was effective in degrading formaldehyde, which is another major pollutant in waste water from a factory producing phenolic resin. The promising result from the bio-treatment of such factory effluent makes Candida albicans TL3 be a potentially useful strain for industrial application.
Synthesis of muconic acids peracetic acid oxidation of catechols
McKague, A. Bruce
, p. 1463 - 1475 (1999)
Monomeric and dimeric muconic acids were prepared in 30-83% yield by oxidation of catechols with peracetic acid in acetic acid.
Monitoring of phenol photodegradation by ultraviolet spectroscopy
Roig, Benoit,Gonzalez,Thomas
, p. 303 - 307 (2003)
Advanced oxidation processes (AOPs) have been developed as an emerging technology for hazardous organic treatment in industrial wastewater. In this paper, the contribution of ultraviolet (UV) spectroscopy to follow phenol photodegradation was studied in a laboratory photochemical reactor equipped with a low pressure mercury lamp. It has been observed that a multicomponent approach is efficient for the evolution estimation of the initial product or intermediate compounds formed during the photodegradation.
Investigation of acid-base catalysis in the extradiol and intradiol catechol dioxygenase reactions using a broad specificity mutant enzyme and model chemistry
Brivio, Michela,Schlosrich, Janne,Ahmad, Mark,Tolond, Caroline,Bugg, Timothy D. H.
, p. 1368 - 1373 (2009)
The extradiol and intradiol catechol dioxygenase reaction mechanisms proceed via a common proximal hydroperoxide intermediate, which is processed via different Criegee 1,2-rearrangements. An R215W mutant of extradiol dioxygenase MhpB, able to produce a mi
High-yield production of cis,cis-muconic acid from catechol in aqueous solution by biocatalyst
Kaneko, Aya,Ishii, Yoshitaka,Kirimura, Kohtaro
, p. 381 - 383 (2011)
A fed-batch process was used to produce cis,cis-muconic acid from catechol by recombinant Escherichia coli cells expressing the catA gene, which encodes the Pseudomonas putida mt-2 catechol 1,2-dioxygenase responsible for catalyzing ortho-cleavage of catechol, as biocatalysts. We succeeded in producing 415mM (59.0 g L-1) cis,cis-muconic acid in aqueous solution without generation of by-products in 12 h under the optimal conditions with successive addition of 10mM catechol. The molar conversion yield based on the amount of consumed catechol was the theoretical value of 100% (mol mol-1).
Cloning and functional analysis of aniline dioxygenase gene cluster, from Frateuria species ANA-18, that metabolizes aniline via an ortho-cleavage pathway of catechol.
Murakami, Shuichiro,Hayashi, Teruhiko,Maeda, Tetsuya,Takenaka, Shinji,Aoki, Kenji
, p. 2351 - 2358 (2003)
Genes encoding an aniline dioxygenase of Frateuria sp. ANA-18, which metabolizes aniline via the ortho-cleavage pathway of catechol, were cloned and named tdn genes. The tdn genes were located on the chromosomal DNA of this bacterium and weren't clustered with catechol-degrading gene clusters. These results show that the ANA-18 aniline-degrading gene cluster is constructionally different from Pseudomonas tdn and Acinetobacter atd gene clusters, which degrade aniline via the meta-cleavage pathway of catechol and organize catechol-metabolic genes in the gene clusters. When cloned tdnQTA1A2B genes were expressed in Eschherichia coli, aniline dioxygenase activity was observed. Southern blot analysis revealed that homologues of the tdnA1A2B genes didn't exist in strain ANA-18. Disruption of the tdnA1A2 genes gave the parent strain ANA-18 a defect in aniline metabolism. On the basis of these results, we concluded that only the cloned tdn genes function as genes encoding aniline dioxygenase in strain ANA-18 although this bacterium had two catechol-degrading gene clusters.
An EPR, thermostability and pH-dependence study of wild-type and mutant forms of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13
Caglio, Raffaella,Pessione, Enrica,Valetti, Francesca,Giunta, Carlo,Ghibaudi, Elena
, p. 75 - 84 (2013)
Intradiol dioxygenase are iron-containing enzymes involved in the bacterial degradation of natural and xenobiotic aromatic compounds. The wild-type and mutants forms of catechol 1,2-dioxygenase Iso B from Acinetobacter radioresistens LMG S13 have been investigated in order to get an insight on the structure-function relationships within this system. 4K CW-EPR spectroscopy highlighted different oxygen binding properties of some mutants with respect to the wild-type enzyme, suggesting that a fine tuning of the substrate-binding determinants in the active site pocket may indirectly result in variations of the iron reactivity. A thermostability investigation by optical spectroscopy, that reports on the state of the metal center, showed that the structural stability is more influenced by the type rather than by the position of the mutation. Finally, the influence of pH and temperature on the catalytic activity was monitored and discussed in terms of perturbations induced on the tertiary contact network of the enzyme. Springer Science+Business Media New York 2013.
