Cytochrome P-450 Involvement in the Oxidation of n-Octane by Cell-free Extracts of Corynebacterium sp. Strain 7E1C

Abstract

Abstract It has been demonstrated that cell-free extracts of Corynebacterium sp. (7E1C) oxidize n-octane to 1-octanol and octanoic acid. This oxidation was catalyzed by a soluble enzyme system and required specifically NADH and molecular O2. It was insensitive to cyanide but it was inhibited by low concentrations of carbon monoxide. The active enzyme system was resolved into two protein fractions by precipitation with ammonium sulfate, and both were required for n-octane oxidation. One fraction exhibited the spectral characteristics of cytochrome P-450 which could be converted to the P-420 form. The other fraction exhibited the spectral characteristic of a flavoprotein.