The Enzyme Database

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Accepted name: nitroarene dioxygenase
Reaction: nitrobenzene + NADH + O2 = catechol + nitrite + NAD+
For diagram of catechol biosynthesis, click here
Other name(s): cnbA (gene name)
Systematic name: nitrobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating, nitrite-releasing)
Comments: This enzyme is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC, ferredoxin—NAD+ reductase), and an α3β3 oxygenase. The enzyme forms of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It can typically act on many different nitroaromatic compounds, including chlorinated species. Enzymes found in different strains may have different substrate preferences. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Parales, J.V., Parales, R.E., Resnick, S.M. and Gibson, D.T. Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the α subunit of the oxygenase component. J. Bacteriol. 180 (1998) 1194–1199. [PMID: 9495758]
2.  Lessner, D.J., Johnson, G.R., Parales, R.E., Spain, J.C. and Gibson, D.T. Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765. Appl. Environ. Microbiol. 68 (2002) 634–641. [DOI] [PMID: 11823201]
3.  Liu, H., Wang, S.J., Zhang, J.J., Dai, H., Tang, H. and Zhou, N.Y. Patchwork assembly of nag-like nitroarene dioxygenase genes and the 3-chlorocatechol degradation cluster for evolution of the 2-chloronitrobenzene catabolism pathway in Pseudomonas stutzeri ZWLR2-1. Appl. Environ. Microbiol. 77 (2011) 4547–4552. [DOI] [PMID: 21602392]
4.  Singh, D., Kumari, A., Ramaswamy, S. and Ramanathan, G. Expression, purification and substrate specificities of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2. Biochem. Biophys. Res. Commun. 445 (2014) 36–42. [DOI] [PMID: 24491551]
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