Results 201 to 210 of about 33,389 (238)

Coniferyl alcohol oxidase ? a catechol oxidase?

Trees, 1995
The 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, RodneyA. Savidge   +1 more
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Tyrosinase and Catechol Oxidase

Nature, 1938
THE 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, 2007
The 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, 2002
A 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, Belle, Catherine, Hamman, Sylvain, Pierre, Jean-Louis, Saint-Aman, Eric   +4 more
openaire   +3 more sources

New functional models for catechol oxidases

Inorganica Chimica Acta, 2000
The 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, Niclas Möller, Bernt Krebs   +2 more
openaire   +1 more source

Olive catechol oxidase ‐ changes during fruit development

Journal of the Science of Food and Agriculture, 1977
AbstractChanges were recorded in the subcellular location of catechol oxidase. In the green olive the enzyme is tightly bound to the chloroplast whereas in the black fruit it is essentially soluble. During fruit development, enzyme activity per fruit declines while the o‐diphenolic content rises steadily.
N, Ben-Shalom, V, Kahn, E, Harel, A M, Mayer   +3 more
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Catechol oxidases, endogenous substrates and browning in developing apples

Journal of the Science of Food and Agriculture, 1966
AbstractThe 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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Catechol oxidase of red delicious apple peel

Phytochemistry, 1972
Abstract 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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Synthetic models of the active site of catechol oxidase: mechanistic studies

Chemical Society Reviews, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Koval, Iryna, Gamez, Patrick, Belle, Catherine, Selmeczi, Katalin, Reedijk, Jan   +4 more
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The selective inhibition of catechol oxidases by salicylhydroxamic acid.

Phytochemistry, 1988
Abstract Salicylhydroxamic acid (SHAM) has been shown to be a powerful and selective inhibitor of catechol oxidases but was without effect on laccases.
Andrew C. Allan, John R.L. Walker
openaire   +1 more source