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Main Title Oxidation of Biphenyl by a Multicomponent Enzyme System from 'Pseudomonas' sp. Strain LB400.
Author Haddock, J. D. ; Nadim, L. M. ; Gibson, D. T. ;
CORP Author Iowa Univ., Iowa City.;Environmental Protection Agency, Cincinnati, OH. Hazardous Waste Engineering Research Lab.
Publisher c1993
Year Published 1993
Report Number EPA-CR-816352; EPA/600/J-93/328;
Stock Number PB93-229466
Additional Subjects Oxidation ; Polychlorinated biphenyls ; Enzyme activity ; Biodegradation ; Chemical reactions ; Microbiology ; Bacteria ; Biochemistry ; Genetics ; Microbiology ; Reprints ; Pseudomonas sp Strain LB400 ; Strains(Biology) ; Congeners
Library Call Number Additional Info Location Last
NTIS  PB93-229466 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 9p
Pseudomonas sp. strain LB400 grows on biphenyl as the sole carbon and energy source. The organism also cooxidizes several chlorinated biphenyl congeners. Biphenyl dioxygenase activity in cell extract required addition of NAD(P)H as an electron donor for the conversion of biphenyl to cis-2,3-dihydroxy-2,3-dihydrobiphenyl. Incorporation of both atoms of molecular oxygen into the substrate was shown with (18)O2. The nonlinear relationship between enzyme activity and protein concentration suggested that the enzyme is composed of multiple protein components. Ion-exchange chromatography of the cell extract gave three protein fractions that were required together to restore enzymatic activity. Similarities with other multicomponent aromatic hydrocarbon dioxygenases indicated that biphenyl dioxygenase may consist of a flavoprotein and iron-sulfur proteins that constitute a short electron transport chain involved in catalyzing the incorporation of both atoms of molecular oxygen into the aromatic ring. (Copyright (c) 1993, American Society for Microbiology.)