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OXIDATION OF BIPHENYL BY A MULTICOMPONENT ENZYME SYSTEM FROM PSEUDOMONAS SP. STRAIN LB400
Citation:
Haddock, J., L. Nadim, AND D. Gibson. OXIDATION OF BIPHENYL BY A MULTICOMPONENT ENZYME SYSTEM FROM PSEUDOMONAS SP. STRAIN LB400. U.S. Environmental Protection Agency, Washington, D.C., EPA/600/J-93/328 (NTIS PB93229466), 1993.
Description:
Pseudomonas sp. strain LB400 grows on biphenyl as the sole carbon and energy source. his organism also cooxidizes several chlorinated biphenyl congeners. iphenyl 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. ncorporation of both atoms of molecular oxygen into the substrate was shown with 18 02. he nonlinear relationship between enzyme activity and protein concentration suggested that the enzyme is composed of multiple protein components. on-exchange chromatography of the cell extract gave three protein fractions that were required together to restore enzymatic activity. imilarities with other multicomponent aromatic hydrocarbon dioxygenases indicated that biphenyl dioxygenase may consist of a flavorprotein and iron-sulfure proteins that constitute a short electron transport chain involved in catalyzing the incorporation of both atoms of molecular oxygen into the aromatic ring.
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OXIDATION OF BIPHENYL BY A MULTICOMPONENT ENZYME SYSTEM FROM PSEUDOMONAS SP. STRAIN LB400