Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)

4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O

4-nitrocatechol [CPD:C02235];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]

Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].

EC 1.14.13.166 created 2012

1  [PMID:9647818]

Kadiyala V, Spain JC

A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus  JS905.

Appl Environ Microbiol 64:2479-84 (1998)
DOI:10.1128/AEM.64.7.2479-2484.1998

2  [PMID:15262926]

Kitagawa W, Kimura N, Kamagata Y

A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101.

J Bacteriol 186:4894-902 (2004)
DOI:10.1128/JB.186.15.4894-4902.2004

[ag:BAD30042 BAD30041]

3  [PMID:19218392]

Zhang JJ, Liu H, Xiao Y, Zhang XE, Zhou NY

Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3.

J Bacteriol 191:2703-10 (2009)
DOI:10.1128/JB.01566-08

[ag:ABU50908]