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

The Biochemical journal ·Vol. 146 ·No. 1 ·1975-01-00 ·Pages 173-83

Axcell BC, Geary PJ

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,metabolism Ultracentrifugation

Chemicals

Bacterial Proteins Flavoproteins NAD Iron Benzene

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Axcell B C

Geary P J

References (10)

10 references, click to expand

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Pufification of a 4-methoxybenzoate O-demethylase from Pseudomonas putida.
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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1460173

Published

1975-01-00

Pages

173-83

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1165286

Subset

External Links

PubMed source DOI: 10.1042/bj1460173 PMC Full Text View journal details

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

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