Results 151 to 160 of about 306,357 (240)
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Synthetic models of the active site of catechol oxidase: mechanistic studies
Chemical Society Reviews, 2006AbstractChemInform 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.
Patrick Gamez +2 more
exaly +4 more sources
Analytical Chemistry, 2023
Expanding sensing modes and improving catalytic performance of nanozyme-based analytical chemistry are beneficial to realizing the desired biosensing of analytes.
Yuechun Li +12 more
semanticscholar +1 more source
Expanding sensing modes and improving catalytic performance of nanozyme-based analytical chemistry are beneficial to realizing the desired biosensing of analytes.
Yuechun Li +12 more
semanticscholar +1 more source
Nano letters (Print), 2023
Developing highly active and selective advanced nanozymes for enzyme-mimicking catalysis remains a long-standing challenge for basic research and practical applications.
Meng Sha +11 more
semanticscholar +1 more source
Developing highly active and selective advanced nanozymes for enzyme-mimicking catalysis remains a long-standing challenge for basic research and practical applications.
Meng Sha +11 more
semanticscholar +1 more source
Analytica Chimica Acta, 2023
In order to effectively monitor multiple catecholamine (CA) neurotransmitters with extreme similar structures, a rapid, sensitive and selective detection strategy has become an urgent problem to be solved.
Jian Yin +5 more
semanticscholar +1 more source
In order to effectively monitor multiple catecholamine (CA) neurotransmitters with extreme similar structures, a rapid, sensitive and selective detection strategy has become an urgent problem to be solved.
Jian Yin +5 more
semanticscholar +1 more source
Journal of coordination chemistry, 2022
Catecholase activity is a biological process in which type-3 active site of a copper enzyme, named catechol oxidase, catalyzes oxidation of o-diphenolic substrates to the corresponding o-quinones coupled with reduction of molecular dioxygen into water ...
R. Tripathy +2 more
semanticscholar +1 more source
Catecholase activity is a biological process in which type-3 active site of a copper enzyme, named catechol oxidase, catalyzes oxidation of o-diphenolic substrates to the corresponding o-quinones coupled with reduction of molecular dioxygen into water ...
R. Tripathy +2 more
semanticscholar +1 more source
International Journal of Biological Macromolecules, 2021
Tyrosinase (Ty) and catechol oxidase (CO) are members of type-3 copper enzymes. While Ty catalyzes both phenolase and catecholase reactions, CO catalyzes only the latter reaction.
Y. Matoba +3 more
semanticscholar +1 more source
Tyrosinase (Ty) and catechol oxidase (CO) are members of type-3 copper enzymes. While Ty catalyzes both phenolase and catecholase reactions, CO catalyzes only the latter reaction.
Y. Matoba +3 more
semanticscholar +1 more source
, 2021
Enzyme-simulating nanomaterials, with obvious advantages of high activity, stability and cost-effectiveness, can surrogate the complex natural enzymes and catalyze enzyme-like reactions in various harsh applications.
Dongxu Zhang +4 more
semanticscholar +1 more source
Enzyme-simulating nanomaterials, with obvious advantages of high activity, stability and cost-effectiveness, can surrogate the complex natural enzymes and catalyze enzyme-like reactions in various harsh applications.
Dongxu Zhang +4 more
semanticscholar +1 more source
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
openaire +1 more source
, 2020
Two ternary copper(II) complexes 1 [(Cu2Me4en)4(EDTA)] and 2 [(CuMe4en)2(MIDA)] containing the mixed ligand system of 1,1′,4,4′-tetramethylethylenediamine (Me4en) (L) and N-methyliminodiacetic (MIDAH2) (L′) or ethylenediaminetetraacetic acid (EDTAH4) (L′)
A. Ramadan +6 more
semanticscholar +1 more source
Two ternary copper(II) complexes 1 [(Cu2Me4en)4(EDTA)] and 2 [(CuMe4en)2(MIDA)] containing the mixed ligand system of 1,1′,4,4′-tetramethylethylenediamine (Me4en) (L) and N-methyliminodiacetic (MIDAH2) (L′) or ethylenediaminetetraacetic acid (EDTAH4) (L′)
A. Ramadan +6 more
semanticscholar +1 more source
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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