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An Efficient Antibody-Catalyzed Oxygenation Reaction
Ist Teil von
Journal of the American Chemical Society, 1994-03, Vol.116 (5), p.2167-2168
Ort / Verlag
Washington, DC: American Chemical Society
Erscheinungsjahr
1994
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Biological oxygen-transfer reactions are essential for the biosynthesis of steroids and neurotransmitters, the degradation of endogenous substances, and the detoxification of xenobiotics. The monooxygenase enzymes responsible for these transformations require biological cofactors such as flavin, heme and non-heme iron, copper, or pterin and typically utilize NADPH for cofactor regeneration. Given their biological and chemical importance, oxygenation reactions have long been targets for antibody catalysis, and in a few cases, redox-active heme and flavin-dependent antibodies have been characterized. More recently, a new strategy has emerged for the generation of catalytic antibodies which utilizes unnatural, chemical cofactors. We now report an antibody-catalyzed sulfide oxygenation reaction mediated by the chemical cofactor sodium periodate, with turnover numbers similar to those of the corresponding enzymatic reactions. (DBO)