Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1 |
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| Affiliation: | 1. Department of Chemistry, Wesleyan University, Middletown, CT 06459, USA;2. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA;1. Department of Chemistry and Environmental Science, New Jersey Institute of Technology, Newark, NJ, USA;2. Department of Civil and Environmental Engineering, Rice University, Houston, TX, USA;3. Research Center of Resource Environment and Urban Planning, Changsha University of Science and Technology, Changsha, Hunan, China;4. CH2M, Englewood, CO, USA;1. Department of Biochemistry, Zunyi Medical University, Zunyi 563000, PR China;2. School of Pharmacy, Zunyi Medical University, Zunyi 563000, PR China;1. Perm State National Research University, 15 Bukirev Str., 614990 Perm, Russia;2. Institute of Ecology and Genetics of Microorganisms, Ural Branch of the Russian Academy of Sciences, 13 Golev Str., 614081 Perm, Russia;3. Institute of Technical Chemistry, Ural Branch of the Russian Academy of Sciences, 3 Acad. Korolev Str., 614013 Perm, Russia |
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| Abstract: | With the aim to enlarge the set of available flavoprotein monooxygenases, we have cloned 8 unexplored genes from Rhodococcus jostii RHA1 that were predicted to encode class B flavoprotein monooxygenases. Each monooxygenase can be expressed as soluble protein and has been tested for conversion of sulfides and ketones. Not only enantioselective sulfoxidations, but also enantioselective Baeyer–Villiger oxidations could be performed with this set of monooxygenases. Interestingly, in contrast to known class B flavoprotein monooxygenases, all studied biocatalysts showed no nicotinamide coenzyme preference. This feature coincides with the fact that the respective sequences appear to form a discrete group of sequence related proteins, distinct from the known class B flavoprotein monooxygenases subclasses: the so-called flavin-containing monooxygenases (FMOs), N-hydroxylating monooxygenases (NMOs) and Type I Baeyer–Villiger monooxygenases (BVMOs). Taken together, these data reveal the existence of a new subclass of class B flavoprotein monooxygenases, which we coined as Type II FMOs, that can perform Baeyer–Villiger oxidations and accept both NADPH and NADH as coenzyme. The uncovered biocatalytic properties of the studied Type II FMOs make this newly recognized subclass of monooxygenases of potential interest for biocatalytic applications. |
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