Mixed regiospecificity compromises alkene synthesis by a cytochrome P450 peroxygenase from Methylobacterium populi

Intensive interest has focused on enzymes that are capable of synthesizing hydrocarbons, alkenes and alkanes, for sustainable fuel production. A recently described cytochrome P450 (OleT(JE)) from the CYP152 family catalyzes an unusual carbon-carbon scission reaction, transforming C-n fatty acids to Cn-1 1-alkenes. Here, we show that a second CYP152, CYP-MP from Methylobacterium populi ATCC BAA 705, also catalyzes oxidative substrate decarboxylation. Alkene production is accompanied with the production of fatty alcohol products, underscoring the mechanistic similarity of the decarboxylation reaction with canonical P450 monooxygenation chemistry. The branchpoint of these two chemistries, and regiospecificity of oxidation products, is strongly chain length dependent, suggesting an importance of substrate coordination for regulating alkene production. (C) 2016 Elsevier Inc. All rights reserved.