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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.
E Harel, A M Mayer
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ChemCatChem, 2013
Enzymatic mimics are designed by using small molecules to impart insight into the mechanistic pathways of the enzymes and to generate catalysts that could be as efficient as the enzyme itself. Among the copper-based polyphenol oxidase enzymes, the copper(II)-containing enzyme catechol oxidase catalyses exclusively the oxidation of ortho-diphenols to ...
Suman Kr Dey, Arindam Mukherjee
exaly +2 more sources
Enzymatic mimics are designed by using small molecules to impart insight into the mechanistic pathways of the enzymes and to generate catalysts that could be as efficient as the enzyme itself. Among the copper-based polyphenol oxidase enzymes, the copper(II)-containing enzyme catechol oxidase catalyses exclusively the oxidation of ortho-diphenols to ...
Suman Kr Dey, Arindam Mukherjee
exaly +2 more sources
, 1994 Oxidation of Catechol by Tea-Oxidase
Nature, 1950DURING the enzymic oxidation of catechol, approximately two atoms of oxygen are taken up for each molecule of catechol, whereas only one atom is required for oxidation to the o-quinone stage. Wagreich and Nelson1 consider this extra uptake to be accounted for by the interaction of the o-benz-quinone with water to form 1 : 2 : 4-trihydroxy-benzene ...
E A H, ROBERTS, D J, WOOD
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Coniferyl alcohol oxidase ? a catechol oxidase?
Trees, 1995The physico-chemical properties of coniferyl alcohol oxidase (CAO), a copper containing glycoprotein spatiotemporally associated with lignification in conifers, is reported here. By electron paramagnetic resonance spectroscopy, only type 3 copper was indicated in CAO. CAO oxidizes several laccase substrates; however, it is not a blue-copper protein and
PreethiV. Udagama-Randeniya +1 more
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Tyrosinase and Catechol Oxidase
Nature, 1938THE nature of tyrosinase has been under discussion for a very long time. Raper and his school1, Graubard and Nelson2, and Keilin and Mann3 believe it to be a distinct enzyme, different from catechol oxidase. Onslow and Robinson4, McCance5, and Richter6 believe it to be a catechol oxidase plus o-chinone plus dehydrogenase. Kubowitz7, whose work appeared
L. CALIFANO, D. KERTESZ
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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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Substrate Binding in Catechol Oxidase Activity: Biomimetic Approach
Inorganic Chemistry, 2002A series of dicopper(II) complexes have been investigated as model systems for the catechol oxidase active site enzyme, regarding the binding of catechol substrate in the first step of the catalytic cycle. The [Cu(2)(L(R))(mu-OH)](ClO(4))(2) and [Cu(2)(L(R))(H(2)O)(2)](ClO(4))(3) complexes are based on the L(R) ligands (2,6-bis[(bis(2-pyridylmethyl ...
Torelli, Stephane +4 more
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New functional models for catechol oxidases
Inorganica Chimica Acta, 2000The new dinuclear copper(II) complexes [Cu2(L1)(m-OAc)](ClO4)2·CH3CN (1), [Cu2(L2)(CH3CN)2](ClO4)4·C2H5OH (2), [Cu2(L3)2(CH3CN)2](PF6)2 (3) and [Cu2(L4)2](PF6)2·2CH2Cl2 (4) were prepared with the ligands N,N,N%,N%-tetrakis((N-2-hydroxyethyl)-2-benzimidazolylmethyl)-2-hydroxy-1,3-diaminopropane HL1, N,N,N%,N%-tetrakis (2-methylimidazolyl)-2-hydroxy-1,3 ...
Pavel Gentschev +2 more
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