nitronate monooxygenase;
NMO;
2-nitropropane dioxygenase (incorrect)

Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2;
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

nitronate:oxygen 2-oxidoreductase (nitrite-forming)

ethylnitronate + O2 = acetaldehyde + nitrite + other products [RN:R00025]

R00025

ethylnitronate [CPD:C18091];
O2 [CPD:C00007]

Previously classified as 2-nitropropane dioxygenase (EC 1.13.11.32), but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Neither hydrogen peroxide nor superoxide were detected during enzyme turnover. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.

1  [PMID:15582992]

Francis K, Russell B, Gadda G.

Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase.

J. Biol. Chem. 280 (2005) 5195-204.

2  [PMID:16682407]

Ha JY, Min JY, Lee SK, Kim HS, Kim do J, Kim KH, Lee HH, Kim HK, Yoon HJ, Suh SW.

Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base.

J. Biol. Chem. 281 (2006) 18660-7.

3  [PMID:19577534]

Gadda G, Francis K

Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in  oxidative catalysis.

Arch. Biochem. Biophys.  (2009) .

4  [PMID:19683782]

Francis K, Gadda G

Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase.

Bioorg. Chem. 37 (2009) 167-72.