Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:15375636, PubMed:15122913). Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS) (PubMed:21048857). an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450] kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150 min(-1) for the reduction of ferricyanide (PubMed:15122913). kcat is 2244 min(-1) for oleic acid hydroxylation (PubMed:15375636). Optimum pH is 7.0. Optimum temperature is 51 degrees Celsius. However, enzyme stability is dramatically reduced at this temperature, incubation for 30 minutes at 31 and 49 degrees Celsius results in 61% and 17% residual activity, respectively. Incubation at 60 degrees Celsius leads to total inactivation of the enzyme. In the N-terminal section; belongs to the cytochrome P450 family.