:Nitronate monooxygenase

{{Infobox enzyme

| Name = Nitronate monooxygenase

| EC_number = 1.13.12.16

| CAS_number =

| GO_code =

| image =

| width =

| caption =

}}

Nitronate monooxygenase ({{EC number|1.13.12.16}}, NMO) is an enzyme with systematic name nitronate:oxygen 2-oxidoreductase (nitrite-forming).{{cite journal | vauthors = Francis K, Russell B, Gadda G | title = Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase | journal = The Journal of Biological Chemistry | volume = 280 | issue = 7 | pages = 5195–204 | date = February 2005 | pmid = 15582992 | doi = 10.1074/jbc.M411249200 | doi-access = free }}{{cite journal | vauthors = Ha JY, Min JY, Lee SK, Kim HS, Kim DJ, Kim KH, Lee HH, Kim HK, Yoon HJ, Suh SW | title = Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base | journal = The Journal of Biological Chemistry | volume = 281 | issue = 27 | pages = 18660–7 | date = July 2006 | pmid = 16682407 | doi = 10.1074/jbc.M601658200 | doi-access = free }}{{cite journal | vauthors = Gadda G, Francis K | title = Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis | journal = Archives of Biochemistry and Biophysics | volume = 493 | issue = 1 | pages = 53–61 | date = January 2010 | pmid = 19577534 | doi = 10.1016/j.abb.2009.06.018 }}{{cite journal | vauthors = Francis K, Gadda G | title = Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase | journal = Bioorganic Chemistry | volume = 37 | issue = 5 | pages = 167–72 | date = October 2009 | pmid = 19683782 | doi = 10.1016/j.bioorg.2009.07.005 }} This enzyme catalyses the following chemical reaction

: ethylnitronate + O₂ $\backslash rightleftharpoons$ acetaldehyde + nitrite + other products

The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii contain non-covalently bound FMN as the cofactor.