Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas

Biochem J. 1975 Jan;146(1):173-83. doi: 10.1042/bj1460173.

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.

MeSH terms

  • Bacterial Proteins / isolation & purification*
  • Benzene / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Flavoproteins / isolation & purification*
  • Iron / metabolism
  • Molecular Weight
  • NAD / metabolism
  • Oxidation-Reduction
  • Pseudomonas / enzymology*
  • Pseudomonas / metabolism
  • Ultracentrifugation

Substances

  • Bacterial Proteins
  • Flavoproteins
  • NAD
  • Iron
  • Benzene