Search results for "Dopachrome"

showing 3 items of 3 documents

Reactions of Flavonoids with o‑Quinones Interfere with the Spectrophotometric Assay of Tyrosinase Activity

2016

Flavonoids are important food components with antioxidant properties and many of them have been described as tyrosinase inhibitors. Oxidation of quercetin, kaempferol, morin, catechin, and naringenin by mushroom tyrosinase and their influence on the oxidation of l-dopa and l-tyrosine was studied. Reaction rates measured spectrophotometrically and by oxygen consumption differed substantially. All tested flavonoids reacted with 4-tert-butyl-o-benzoquinone and/or 4-methyl-o-benzoquinone, although at different rates. These reactions generated products whose UV-vis spectra either overlapped or did not overlap with the spectrum of dopachrome. They therefore strongly influence the kinetic analysis…

0301 basic medicineNaringenino-quinoneAntioxidantAgaricusTyrosinasemedicine.medical_treatmentMorintyrosinase01 natural sciencesFungal Proteins03 medical and health scienceschemistry.chemical_compoundBenzoquinonesmedicineOrganic chemistryenzymatic assay interferenceEnzyme AssaysCatecholMonophenol Monooxygenase010401 analytical chemistryfood and beveragesCatechinGeneral Chemistrycatechol0104 chemical sciencesKinetics030104 developmental biologychemistrySpectrophotometryflavonoidsDopachromeredox exchangeGeneral Agricultural and Biological SciencesKaempferolOxidation-ReductionNuclear chemistryJournal of Agricultural and Food Chemistry
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Redox reaction between amino-(3,4-dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosin…

2002

Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid, the phosphonic analog of 3,4-dihydroxyphenylglycine, had been previously reported as a potent inhibitor of tyrosinase. The mechanism of the apparent enzyme inhibition by this compound has now been established. Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid turned out to be a substrate and was oxidized to o-quinone, which evolved to a final product identified as 3,4-dihydroxybenzaldehyde, the same as for 3,4-dihydroxyphenylglycine. Monohydroxylated compounds (amino-(3-hydroxyphenyl)methyl phosphonic acid and amino-(4-hydroxyphenyl)methyl phosphonic acid) were not oxidized, neither was 4-hydroxy-l-phenylglycine. However, the relatively hig…

Alaninechemistry.chemical_compoundNon-competitive inhibitionChemistryStereochemistryTyrosinaseDopachromeSubstrate (chemistry)TyrosineBiochemistryRedoxQuinoneEuropean Journal of Biochemistry
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Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

2011

The vanadium haloperoxidase (V-HPO) enzyme, extracted from the brown alga Laminaria saccharina, is able to catalyze the formation of a black precipitate, using as precursor the amino acid L-dopa in the presence of hydrogen peroxide and iodide, in one-pot synthesis. The L-dopa oxidation is a multistep reaction with a crucial role played by the iodide in the enzyme catalyzed peroxidative production of dopachrome, a well known intermediate in the synthesis of melanin. Dopachrome is then converted to a synthetic form of melanin through a polymerization reaction. Factors, such as buffer composition and pH, influence significantly the reaction first steps, but further steps of melanin production …

Protein ConformationTyrosinaseIodideBuffersBiochemistryPolymerizationLevodopaInorganic ChemistryMelaninchemistry.chemical_compoundHaloperoxidaseOrganic chemistryIndolequinonesHydrogen peroxideMelaninschemistry.chemical_classificationChemistryVanadiumHydrogen PeroxideHydrogen-Ion ConcentrationIodidesKineticsPeroxidasesPolymerizationBiocatalysisBiocatalysisMicroscopy Electron ScanningDopachromeJournal of Inorganic Biochemistry
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