Purification and some properties of a soluble benzene-oxidizing system from a strain of <i>Pseudomonas</i>

Abstract

1. A soluble enzyme system which oxidizes benzene to cis-1,2-dihydroxycyclohexa-3,5-diene (cis-benzene glycol) was obtained from a species of Pseudomonas grown on benzene as the major carbon source. 2. The system was shown to consist of three protein components. Two of these were non-haem-iron proteins of molecular weight approx. 21,000 and approx. 186,000 and the other was a flavoprotein of molecular weight approx. 60,000. 3. Fe2+ and NADH were essential cofactors for benzene oxidation.