Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas.
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.
D001426:Bacterial Proteins / Q000302:isolation & purification*; D001554:Benzene / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005420:Flavoproteins / Q000302:isolation & purification*; D007501:Iron / Q000378:metabolism; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology* / Q000378:metabolism; D014461:Ultracentrifugation
D001426:Bacterial Proteins; D005420:Flavoproteins; D009243:NAD; D007501:Iron; D001554:Benzene