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Applied and Environmental Microbiology, February 2008, p. 1050-1057, Vol. 74, No. 4
0099-2240/08/$08.00+0 doi:10.1128/AEM.01627-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Unité de Génie Biologique,1 Unité de Génétique, Institut des Sciences de la Vie, Université Catholique de Louvain, Place Croix du Sud, 2/19, B-1348 Louvain-la-Neuve, Belgium,4 Biotechnology Center for Agriculture and the Environment, Cook College, Rutgers University, New Brunswick, New Jersey,2 Laboratoire de Chimie et Biologie des Métaux, iRTSV, CEA, CNRS, Université J. Fourier UMR 5249, CEA-Grenoble, F-38054 Grenoble Cedex 9, France3
Received 17 July 2007/ Accepted 14 December 2007
In this study, the genes involved in the initial attack on fluorene by Sphingomonas sp. strain LB126 were investigated. The
and β subunits of a dioxygenase complex (FlnA1-FlnA2), showing 63 and 51% sequence identity, respectively, to the subunits of an angular dioxygenase from the gram-positive dibenzofuran degrader Terrabacter sp. strain DBF63, were identified. When overexpressed in Escherichia coli, FlnA1-FlnA2 was responsible for the angular oxidation of fluorene, 9-hydroxyfluorene, 9-fluorenone, dibenzofuran, and dibenzo-p-dioxin. Moreover, FlnA1-FlnA2 was able to oxidize polycyclic aromatic hydrocarbons and heteroaromatics, some of which were not oxidized by the dioxygenase from Terrabacter sp. strain DBF63. The quantification of resulting oxidation products showed that fluorene and phenanthrene were the preferred substrates of FlnA1-FlnA2.
Published ahead of print on 21 December 2007.
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