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• W2090673485 startingPage "2815" @default.
• W2090673485 abstract "A structural and functional mimic of the galactose oxidase (GOase) enzyme active-site by a copper complex supported over a sterically demanding ligand having [N2O2] donor sites is reported. Specifically, the binding of the histidine (496 and 581) and tyrosine (272 and 495) residues to the copper center in a square-pyramidal fashion in the active-site of galactose oxidase (GOase) enzyme has been modeled in a copper complex, {[(3-tert-butyl-5-methyl-2-hydoxybenzyl)(3′-tert-butyl-5′-methyl-2′-oxobenzyl)(2-pyridylmethyl)]amine}Cu(OAc)} (1b), stabilized over a sterically demanding ligand in which the two phenolate-O atoms mimicked the tyrosine binding while an amine-N and pyridyl-N atoms emulated the histidine binding to the metal center, similar to that in the enzyme active-site. Furthermore, the copper complex 1b is found to be an effective functional model of the enzyme as it efficiently catalyzed the chemoselective oxidation of primary alcohols to aldehydes in high turnover numbers under ambient conditions. An insight into the nature of the active-species was obtained by EPR and CV studies, which in conjunction with the DFT studies, revealed that the active-species is an anti-ferromagnetically coupled diamagnetic radical cation, 11b+, obtained by one electron oxidation at the equatorial phenolate-O atom of the ligand in the 1b complex." @default.
• W2090673485 created "2016-06-24" @default.
• W2090673485 creator A5026949597 @default.
• W2090673485 creator A5053722424 @default.
• W2090673485 creator A5074427160 @default.
• W2090673485 date "2008-01-01" @default.
• W2090673485 modified "2023-10-11" @default.
• W2090673485 title "Structural and functional mimic of galactose oxidase by a copper complex of a sterically demanding [N2O2] ligand" @default.
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• W2090673485 doi "https://doi.org/10.1039/b801496e" @default.
• W2090673485 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18478142" @default.
• W2090673485 hasPublicationYear "2008" @default.
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