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. 1974 Sep;119(3):879–888. doi: 10.1128/jb.119.3.879-888.1974

Purification and Propeties of (+)-cis-Naphthalene Dihydrodiol Dehydrogenase of Pseudomonas putida

T R Patel 1, D T Gibson 1
PMCID: PMC245694  PMID: 4369091

Abstract

Cells of Pseudomonas putida, after growth with naphthalene as sole source of carbon and energy, contain an enzyme that oxidizes (+)-cis-1(r),2(s)-dihydroxy-1,2-dihydronaphthalene to 1,2-dihydroxynaphthalene. The purified enzyme has a molecular weight of 102,000 and apparently consists of four 25,500 molecular weight subunits. The enzyme is specific for nicotinamide adenine dinucleotide as an electron acceptor and also oxidizes several other cis-dihydrodiols. However, no enzymatic activity was observed with trans-1,2-dihydronaphthalene, or the K-region cis-dihydrodiols of carcinogenic polycyclic hydrocarbons.

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