In vitro study demonstrates efficient sulfide oxygenation by a catalytic antibody using sodium periodate, suggesting viable alternatives to biological monooxygenase cofactors.
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 biological cofactors such as flavin, heme and nonheme , copper, or pterin and typically utilize NADPH for regeneration. Given their biological and chemical , oxygenation reactions have long been targets for catalysis, and in a few cases, redox-active heme and -dependent antibodies have been characterized. More , a new strategy has emerged for the generation of catalytic which utilizes unnatural, chemical cofactor. We report an antibody-catalyzed sulfide oxygenation reaction by the chemical cofactor sodium periodate, with turnover similar to those of the corresponding enzymatic reactions (Scheme 1).
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Hsieh et al. (1994) studied this question.
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