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• W2016040453 abstract "New anionic metalloporphyrin–estradiol conjugates have been synthesized and fully characterized, and have been further associated to a monoclonal anti-estradiol antibody 7A3, to generate new artificial metalloenzymes following the so-called ‘Trojan Horse’ strategy. The spectroscopic characteristics and dissociation constants of these complexes were similar to those obtained for the artificial metalloproteins obtained by association of cationic metalloporphyrin–estradiol conjugates to 7A3. This demonstrates that the nature of the porphyrin substituents, anionic or cationic, had little influence on the association with the antibody that is mainly driven by the tight association of the estradiol anchor with the binding pocket of the antibody. These new biocatalysts appeared to have an interesting catalytic activity in oxidation reactions. The iron(III)–anionic-porphyrin–estradiol-antibody complexes were found able to catalyze the chemoselective and slightly enantioselective (ee = 10%) sulfoxidation of sulfides by H2O2. The Mn(III)–porphyrin–estradiol-antibody complexes were found to catalyze the oxidation of styrene by KHSO5, the Mn(III)–cationic-porphyrin–estradiol-antibody complexes even showing the highest yields so far reported for the oxidation of styrene catalyzed by artificial metalloproteins. However, a lack of chemoselectivity and enantioselectivity was observed, which was probably due to a weak interaction of the metalloporphyrin cofactor with the binding pocket of antibody 7A3, as suggested by the similar UV–visible characteristics and catalytic activities obtained with both anionic and cationic porphyrins." @default.
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• W2016040453 date "2010-06-01" @default.
• W2016040453 modified "2023-09-30" @default.
• W2016040453 title "Oxidation of organic molecules in homogeneous aqueous solution catalyzed by hybrid biocatalysts (based on the Trojan Horse strategy)" @default.
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• W2016040453 doi "https://doi.org/10.1016/j.tetasy.2010.03.050" @default.
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