Functional group diversity in enzymic oxygenation reactions catalyzed by bacterial flavin-containing cyclohexanone oxygenase
- 1 April 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 107 (7) , 2153-2161
- https://doi.org/10.1021/ja00293a054
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The oxidative half-reaction of liver microsomal FAD-containing monooxygenase.Published by Elsevier ,2021
- The reductive half-reaction of liver microsomal FAD-containing monooxygenase.Published by Elsevier ,2021
- Monooxygen donation potential of 4a-hydroperoxyflavins as compared with those of a percarboxylic acid and other hydroperoxides. Monooxygen donation to olefin, tertiary amine, alkyl sulfide, and iodide ionJournal of the American Chemical Society, 1983
- Studies on the chirality of sulfoxidation catalyzed by bacterial flavoenzyme cyclohexanone monooxygenase and hog liver FAD-containing monooxygenaseBiochemistry, 1982
- Mechanistic studies on cyclohexanone oxygenaseBiochemistry, 1982
- Dioxygen transfer from 4a-hydroperoxyflavin anion. 4. Dioxygen transfer to phenolate anion as a means of aromatic hydroxylationJournal of the American Chemical Society, 1982
- Mechanism-based enzyme inactivation using an allyl sulfoxide-allyl sulfenate ester rearrangementJournal of the American Chemical Society, 1980
- Kinetic studies on the reaction of p-hydroxybenzoate hydroxylase. Agreement of steady state and rapid reaction data.Journal of Biological Chemistry, 1979
- Structure of the oxygen adduct intermediate in the bacterial luciferase reaction: 13 C nuclear magnetic resonance determinationProceedings of the National Academy of Sciences, 1978
- Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.Journal of Biological Chemistry, 1976