CYP153A71 from Alcanivorax dieselolei: Oxidation beyond Monoterminal Hydroxylation of n-Alkanes

Selective oxyfunctionalization of non-activated C–H bonds remains a major challenge in synthetic chemistry. The biocatalytic hydroxylation by cytochrome P450 monooxygenases (CYPs), however, offers catalysis with high regio- and stereoselectivity using molecular oxygen. CYP153s are class CYPs known for their selective terminal n-alkanes microorganisms, such as the bacterium Alcanivorax dieselolei, have evolved extensive enzymatic pathways various lengths n-alkanes, including CYP153 to yield medium-chain 1-alkanols. In this study, we report characterization alkane hydroxylase from A. dieselolei (CYP153A71) comparison well-known CYP153A6 CYP153A13. Although expected 1-alkanols produced, CYP153A71 readily converts corresponding aldehydes, fatty acids, well ?,?-diols. is also shown hydroxylate acids. X-ray crystal structure bound octanoic acid solved, yielding an insight into not only regioselectivity, but binding orientation substrate, which can be used future studies evolve improved oxidations beyond n-alkane hydroxylation.