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. 1975 Jan;146(1):173–183. doi: 10.1042/bj1460173

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

B C Axcell, P J Geary
PMCID: PMC1165286  PMID: 167712

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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