Abstract
1. cis-Benzene glycol dehydrogenase was purified to a homogeneous state from a species of Pseudomonas grown with benzene as the major carbon source. 2. The enzyme was specific for the cis-isomer of its substrate and required NAD(+) as hydrogen acceptor. 3. Partial inactivation of the enzyme, which was observed during purification, could be reversed by the addition of Fe(2+) and GSH. 4. A molecular weight of 440000 was calculated from data obtained by sedimentation-velocity and diffusion analysis in the ultracentrifuge. Sodium dodecyl sulphate polyacrylamide-gel electrophoresis indicated a subunit of molecular weight 110000. 5. p-Chloromercuribenzoic acid and 1,10-phenanthroline were shown to inhibit the enzyme.
MeSH terms
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Alcohol Oxidoreductases / antagonists & inhibitors
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Benzene / metabolism*
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Cell-Free System
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Chloromercuribenzoates / pharmacology
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Chromatography, DEAE-Cellulose
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Cyclohexanols
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Diffusion
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation
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Glutathione / pharmacology
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Hydrogen-Ion Concentration
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Iron / pharmacology
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Isomerism
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Molecular Weight
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NAD
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Oxidoreductases / isolation & purification*
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Oxidoreductases Acting on CH-CH Group Donors
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Phenanthrolines / pharmacology
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Pseudomonas / enzymology*
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Sodium Dodecyl Sulfate
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Ultracentrifugation
Substances
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Chloromercuribenzoates
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Cyclohexanols
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Phenanthrolines
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NAD
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Sodium Dodecyl Sulfate
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Iron
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Oxidoreductases
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Alcohol Oxidoreductases
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Oxidoreductases Acting on CH-CH Group Donors
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cis-1,2-dihydrobenzene-1,2-diol dehydrogenase
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Glutathione
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Benzene