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ChemCatChem
In nature, catechol oxidase catalyzes the oxidation of o‐diphenol to o‐quinone to produce a series of highly important polyphenolic natural products.
Ajit Kumar Singh +7 more
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In nature, catechol oxidase catalyzes the oxidation of o‐diphenol to o‐quinone to produce a series of highly important polyphenolic natural products.
Ajit Kumar Singh +7 more
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Catechol oxidase of red delicious apple peel
Phytochemistry, 1972Abstract Catechol oxidase has been solubilized from the particulate fraction of apple peel using Triton X-100, dialysis and butanol extraction. The partially purified enzyme retained activity during lyophilization in the presence of mercaptobenzothiazole. The substrate specificity and pH optima of the enzyme are reported.
David A. Stelzig, S. Akhtar, S. Ribeiro
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Inorganica Chimica Acta, 2018
A new cobalt(III) complex, [Co(L-κ-N,N,O)(L-κ-N,O)(NCS)]·0.5H 2 O, with a pendant Schiff base {HL = 2((2-morpholinoethylimino)methyl)-6-ethoxyphenol} has been synthesized and characterized by elemental and several spectral analyses.
Kousik Ghosh, M. Drew, S. Chattopadhyay
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A new cobalt(III) complex, [Co(L-κ-N,N,O)(L-κ-N,O)(NCS)]·0.5H 2 O, with a pendant Schiff base {HL = 2((2-morpholinoethylimino)methyl)-6-ethoxyphenol} has been synthesized and characterized by elemental and several spectral analyses.
Kousik Ghosh, M. Drew, S. Chattopadhyay
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Inorganica Chimica Acta, 2019
A new class of aminophenol ligands, bis(5-(tert-butyl)-2-hydroxybenzyl)glycine (H3L1) and bis(2-hydroxy-5-methylbenzyl)glycine (H3L2) were synthesized by the Mannich reaction.
S. Indira +5 more
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A new class of aminophenol ligands, bis(5-(tert-butyl)-2-hydroxybenzyl)glycine (H3L1) and bis(2-hydroxy-5-methylbenzyl)glycine (H3L2) were synthesized by the Mannich reaction.
S. Indira +5 more
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The catalytic cycle of catechol oxidase
JBIC Journal of Biological Inorganic Chemistry, 2004Hybrid density functional theory with the B3LYP functional has been used to investigate the catalytic mechanism of catechol oxidase. Catechol oxidase belongs to a class of enzymes that has a copper dimer with histidine ligands at the active site. Another member of this class is tyrosinase, which has been studied by similar methods previously.
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Multiple forms of Vitis vinifera catechol oxidase
Phytochemistry, 1973Abstract Grape catechol oxidase shows multiple forms upon ion exchange chromatography, acrylamide gel electrophoresis and gel filtration. Conversion of some bands into others, which occurs during isolation and storage, is enhanced by dilution and by treatment with urea or acid pH.
Eitan Harel +2 more
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Polyhedron, 2018
A mononuclear Co(III) complex [CoL2]Cl (1) [HL = (E)-2-((3-(2-hydroxyethylthio)propylimino)methyl)phenol] was synthesized and its X-ray crystallographic characterization revealed a distorted octahedral geometry around the metal centre.
A. K. Ghosh, C. Purohit, Rajarshi Ghosh
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A mononuclear Co(III) complex [CoL2]Cl (1) [HL = (E)-2-((3-(2-hydroxyethylthio)propylimino)methyl)phenol] was synthesized and its X-ray crystallographic characterization revealed a distorted octahedral geometry around the metal centre.
A. K. Ghosh, C. Purohit, Rajarshi Ghosh
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Theoretical study of the catalytic mechanism of catechol oxidase
JBIC Journal of Biological Inorganic Chemistry, 2007The mechanism for the oxidation of catechol by catechol oxidase has been studied using B3LYP hybrid density functional theory. On the basis of the X-ray structure of the enzyme, the molecular system investigated includes the first-shell protein ligands of the two metal centers as well as the second-shell ligand Cys92.
Mireia, Güell, Per E M, Siegbahn
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Catechol oxidases, endogenous substrates and browning in developing apples
Journal of the Science of Food and Agriculture, 1966AbstractThe content of o‐diphenols and catechol oxidase activity was followed in developing apples from fruit set to harvest time. Afterwards their level drops, apparently due to conversion to other compounds and cessation of synthesis. Catechol oxidase activity shows a peak after that occurring in content of o‐diphenols.
E, Harel, A M, Mayer, Y, Shain
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Unraveling Substrate Specificity and Catalytic Promiscuity of Aspergillus oryzae Catechol Oxidase
ChemBioChem, 2018Catechol oxidases and tyrosinases are coupled binuclear copper enzymes that oxidize various o‐diphenolic compounds to corresponding o‐quinones. Tyrosinases have an additional monooxygenation ability to hydroxylate monophenol to o‐diphenol.
Leena Penttinen +4 more
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