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J. Bacteriol. doi:10.1128/JB.00654-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Molecular Characterization of a Novel ortho-Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215

State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China; Graduate School, Chinese Academy of Sciences, Beijing, 100049, China

^* To whom correspondence should be addressed. Email: n.zhou{at}pentium.whiov.ac.cn.

	Abstract

Alcaligenes sp. strain NyZ215, has been isolated for its ability to grow on ortho-nitrophenol (ONP) as the sole source of carbon, nitrogen and energy, and shown to degrade ONP via a catechol ortho-cleavage pathway. A DNA fragment of 10,152 bp extending from a conserved region of the catechol 1,2-dioxygenase gene was obtained by genome walking. Among 7 complete open reading frames deduced from this fragment, three (onpABC) have been shown to encode the enzymes involved in the initial reactions of o-nitrophenol catabolism in this strain. OnpA, which shares 26% identity with salicylate 1-monooxygenase of Pseudomonas stutzeri AN10, is an ONP 2-monooxygenase (EC 1.14.13.31) which converts ONP to catechol in the presence of NADPH, with concomitant nitrite release. OnpC is a catechol 1,2-dioxygenase catalyzing the oxidation of catechol to cis, cis-muconic acid. OnpB exhibits 54% identity with the reductase subunit of vanillate-O-demethylase in Pseudomonas fluorescens BF13. OnpAB (but not OnpA alone) conferred on the catechol utilizer Pseudomonas putida PaW340 the ability to grow on ONP. This suggests that OnpB may also be involved in ONP degradation in vivo as an o-benzoquinone reductase converting o-benzoquinone to catechol. This is analogous to the reduction of tetrachlorobenzoquinone to tetrachlorohydroquinone by a tetrachlorobenzoquinone reductase (PcpD, 38% identity with OnpB) in the pentachlorophenol degrader Sphingobium chlorophenolicum ATCC39723.

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