An Efficient Antibody-Catalyzed Oxygenation Reaction

Abstract

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 nonheme 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 cofactor. 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 (Scheme 1).

Additional Information

© 1994 American Chemical Society. Financial support was provided by the Assistant Secretary for Conservation and Renewable Energy, Advanced Industrial Concepts Division of the U.S. Department of Energy under Contract No. DE-AC03-76SF00098. L.C.H. gratefully acknowledges the support of the NSF (1990-1993) and SmithKline Beecham for an ACS Organic Chemistry Graduate Fellowship (1993-1994).

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