US EPA

1469870 

Journal Article 

Oxidation of naphthalene by a multicomponent enzyme system from Pseudomonas sp. strain NCIB 9816 

Ensley, BD; Gibson, DT; Laborde, AL 

1982 

Yes 

Journal of Bacteriology
ISSN: 0021-9193
EISSN: 1098-5530 

149 

3 

948-954 

English 

7037744 

10.1128/jb.149.3.948-954.1982 

WOS:A1982NE93700018 

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The initial reactions in the oxidation of naphthalene by Pseudomonas sp. strain NCIB 9816 involves the enzymatic incorporation of one molecule of oxygen into the aromatic nucleus to form (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The enzyme catalyzing this reaction, naphthalene dioxygenase, was resolved into three protein components, designated A, B, and C, by DEAE-cellulose chromatography. Incubation of naphthalene with components A, B, and C in the presence of NADH resulted in the formation of (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The ratio of oxygen and NADH utilization to product formation was 1:1:1. NADPH also served as an electron donor for naphthalene oxygenation. However, its activity was less than 50% of that observed with NADH. Component A showed NAD(P)H-cytochrome c reductase activity which was stimulated by the addition of flavin adenine dinucleotide and flavin mononucleotide. A similar stimulation was observed when these flavin nucleotides were added to the naphthalene dioxygenase assay system. These preliminary observations indicate that naphthalene dioxygenase has properties in common with both monooxygenase and dioxygenase multicomponent enzyme systems. 

strains; components; naphthalene; naphthalene dioxygenase; Microbiology Abstracts B: Bacteriology; Microbiology Abstracts A: Industrial & Applied Microbiology; oxidation; Pseudomonas; A 01016:Microbial degradation; J 02722:Biodegradation, growth, nutrition and leaching