Characterization of a novel angular dioxygenase from fluorene-degrading Spingomonas sp strain LB126

被引:34
作者
Schuler, Luc [1 ]
Chadhain, Sinead M. Ni [2 ]
Jouanneau, Yves [3 ]
Meyer, Christine [3 ]
Zylstra, Gerben J. [2 ]
Hols, Pascal [4 ]
Agathos, Spiros N. [1 ]
机构
[1] Catholic Univ Louvain, Inst Sci Vie, Unite Genie Biol, B-1348 Louvain, Belgium
[2] Catholic Univ Louvain, Unite Genet, B-1348 Louvain, Belgium
[3] Rutgers State Univ, Cook Coll, Biotechnol Ctr Agr & Environm, New Brunswick, NJ USA
[4] Univ Grenoble 1, CEA, Lab Chim Biol Metaux, UMR 5249, F-38054 Grenoble, France
关键词
D O I
10.1128/AEM.01627-07
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
In this study, the genes involved in the initial attack on fluorene by Sphingomonas sp. strain LB126 were investigated. The alpha and beta 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.
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收藏
页码:1050 / 1057
页数:8
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