We are particularly interested in two-component flavin monooxygenases, both because they are systems with strong potential for biotechnological development, and because they are being studied in the laboratory. They consist of a flavin reductase which produces free reduced flavins. These are taken up by the monooxygenase partner, where they react with atmospheric oxygen to produce a flavin hydroperoxide intermediate, which is responsible for substrate oxidation. These enzymes are ubiquitous and are involved in a wide range of oxidation reactions in cells (bacterial in particular). We show two reactions catalyzed by these monooxygenases, which have been the subject of extensive research, including at industrial level: the oxidation of sulfur compounds in the context of the development of petroleum desulfurization processes; and the epoxidation of styrenes to obtain enantiomerically pure epoxides.
This lecture also discusses the case of Baeyer-Villigerases, one-component flavin monooxygenases which catalyze the stereoselective conversion of cyclic ketones to lactones, a highly useful reaction for the chemical industry. After a presentation of the structures and mechanisms of action of this class of enzymes, we show what biotechnological developments are expected (terpenoid and steroid oxidation systems and asymmetric transformations).
