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

Abstract:

:Pseudomonas sp. strain LB400 grows on biphenyl as the sole carbon and energy source. This 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 18O2. 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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Haddock JD,Nadim LM,Gibson DT

doi

10.1128/jb.175.2.395-400.1993

subject

Has Abstract

pub_date

1993-01-01 00:00:00

pages

395-400

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

175

pub_type

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