The heme domain and holoprotein of the self-sufficient Krac9955 enzyme have been purified. The substrate range of Krac9955 has been characterised. A preference for alkyloxy- and alkyl-benzoic acids over fatty acid substrates was observed. The Krac9955 enzyme has a preference for oxidation eight carbons from the carboxylate group. Unusually for a self-sufficient P450 fusion protein the activity of the purified enzyme is low.