Journal
CHEMICAL COMMUNICATIONS
Volume 51, Issue 90, Pages 16173-16175Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5cc06078h
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Funding
- European Research Council (ERC) [297503]
- Deutsche Forschungsgemeinschaft (DFG) through the cluster of excellence Unifying Concepts in Catalysis, Berlin
- Deutscher Akademischer Austauschdienst (DAAD)
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An in vivo biotransformation system is presented that affords the hydroxylation of n-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD(+)-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H-2-driven NADH cofactor regeneration even in the presence of O-2, the co-substrate of monooxygenase.
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