Efficient antibody-catalyzed oxygenation reaction
- Univ. of California, Berkeley, CA (United States)
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. 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. Sodium periodate NaIO[sub 4]O was chosen as the oxidant, since sulfoxide formation occurs under mild aqueous conditions with minimal overoxidation to the sulfone. Furthermore, compared to the flavin and heme cofactors required by the monooxygenase enzymes, NaIO[sub 4] is very inexpensive, obviating the need for cofactor recycling. Overall, these results raise the possibility of using antibodies as catalysts for regio- and stereoselective sulfide oxidations. 18 refs., 1 fig.
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 7162914
- Journal Information:
- Journal of the American Chemical Society; (United States), Vol. 116:5; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
SULFIDES
CHEMICAL REACTION KINETICS
OXIDATION
ANTIBODIES
AROMATICS
CATALYSIS
PERIODATES
SODIUM COMPOUNDS
ALKALI METAL COMPOUNDS
CHALCOGENIDES
CHEMICAL REACTIONS
HALOGEN COMPOUNDS
IODINE COMPOUNDS
KINETICS
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
REACTION KINETICS
SULFUR COMPOUNDS
550200* - Biochemistry
400201 - Chemical & Physicochemical Properties