Oxidation of biphenyl by a multicomponent enzyme system from pseudomonas sp. strain LB400

Technical Report · Fri Jan 01 04:00:00 EST 1993

OSTI ID:5957722

Haddock, J D; Nadim, L M; Gibson, D T

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.

• Research Organization: Iowa Univ., Iowa City, IA (United States)
• OSTI ID: 5957722
• Report Number(s): PB-93-229466/XAB; CNN: EPA-CR-816352
• Country of Publication: United States
• Language: English

Related Subjects

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59 BASIC BIOLOGICAL SCIENCES
AROMATICS
BACTERIA
BIOCHEMISTRY
BIODEGRADATION
BIOLOGY
CHEMICAL REACTIONS
CHEMISTRY
CHLORINATED AROMATIC HYDROCARBONS
DECOMPOSITION
ENZYME ACTIVITY
ENZYMES
GENETICS
HALOGENATED AROMATIC HYDROCARBONS
MICROORGANISMS
ORGANIC CHLORINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
OXIDATION
OXIDOREDUCTASES
OXYGENASES
POLYCHLORINATED BIPHENYLS
PROTEINS
PSEUDOMONAS