H2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase

Abstract

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 H₂-driven NADH cofactor regeneration even in the presence of O₂, the co-substrate of monooxygenase.