PMID:11856757

Adak S, Aulak KS, Stuehr DJ

Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis.

J Biol Chem 277:16167-71 (2002)
DOI:10.1074/jbc.M201136200

[bsu:BSU07630]

PMID:18316370

Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E

Bacterial nitric-oxide synthases operate without a dedicated redox partner.

J Biol Chem 283:13140-7 (2008)
DOI:10.1074/jbc.M710178200

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

L-arginine,reduced-flavodoxin:oxygen oxidoreductase (nitric-oxide-forming)

2 L-arginine + 3 reduced flavodoxin + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O (overall reaction) [RN:R11711];
(1a) 2 L-arginine + 2 reduced flavodoxin + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O  [RN:R11712];
(1b) 2 Nomega-hydroxy-L-arginine + reduced flavodoxin + 2 O2 = 2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O [RN:R11713]

R11711 R11712 R11713
Reaction

L-arginine [CPD:C00062];
reduced flavodoxin [CPD:C02745];
O2 [CPD:C00007];
Nomega-hydroxy-L-arginine [CPD:C05933]

Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. The enzyme, found in bacteria and archaea, consist of only an oxygenase domain and functions together with bacterial ferredoxins or flavodoxins. The orthologous enzymes from plants and animals also contain a reductase domain and use only NADPH as the electron donor (cf. EC 1.14.13.39).

EC 1.14.14.47 created 2012 as EC 1.14.13.165, transferred 2017 to EC 1.14.14.47

1  [PMID:12220171]

Pant K, Bilwes AM, Adak S, Stuehr DJ, Crane BR

Structure of a nitric oxide synthase heme protein from Bacillus subtilis.

Biochemistry 41:11071-9 (2002)
DOI:10.1021/bi0263715

[bsu:BSU07630]

2  [PMID:11856757]

Adak S, Aulak KS, Stuehr DJ

Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis.

J Biol Chem 277:16167-71 (2002)
DOI:10.1074/jbc.M201136200

3  [PMID:17127770]

Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ

Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.

J Biol Chem 282:2196-202 (2007)
DOI:10.1074/jbc.M608206200

4  [PMID:19805284]

Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA

NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum.

Proc Natl Acad Sci U S A 106:16221-6 (2009)
DOI:10.1073/pnas.0908443106

5  [PMID:25194416]

Holden JK, Lim N, Poulos TL

Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.