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2 L-arginine + 2 reduced flavodoxin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O
-
-
-
?
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
2 Nomega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
-
in single turnover experiments with Nomega-hydroxy-L-arginine, NO forms only in the presence of (6R)-tetrahydro-L-biopterin
-
?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
additional information
?
-
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
-
-
-
?
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
-
-
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
-
flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
-
-
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
-
flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
-
overall reaction. Flavodoxins YkuN and YkuP support catalysis as kinetically competent redox partners. When an NADPH-utilizing bacterial flavodoxin reductase is added to reduce YkuP or YkuN, both support nitric oxide synthesis from either L-arginine or N-hydroxyarginine, with YkuN being more efficient
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
-
-
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
tetrahydrobiopterin or tetrahydrofolate may act as redox partners
overall reaction
-
?
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
-
overall reaction
-
?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
-
-
-
?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
-
-
-
?
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
-
-
-
?
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
-
-
-
?
additional information
?
-
ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS
-
-
?
additional information
?
-
NO production requires flavodoxin YkuN and a flavodoxin reductase, YumC fulfilling this requirement
-
-
?
additional information
?
-
ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS
-
-
?
additional information
?
-
NO production requires flavodoxin YkuN and a flavodoxin reductase, YumC fulfilling this requirement
-
-
?
additional information
?
-
-
the complex between enzyme and the unusual tryptophanyl-tRNA synthetase TrpRS II catalyzes the regioselective nitration of tryptophan at the 4-position. The enzyme alone will catalyze 4-nitrotryptophan production, but yields are significantly enhanced by TrpRS II and ATP. 4-Nitro-tryptophan formation exhibits saturation behavior with tryptophan and is completely inhibited by the addition of the mammalian nitric-oxide synthase cofactor (6R)-5,6,7,8-tetrahydro-L-biopterin
-
-
?
additional information
?
-
addition of oxygen to ferrous NOS results in long-lived heme-oxy complexes in the presence (Soret peak 427 nm) and absence (Soret peak 413 nm) of substrates L-arginine and Nomega-hydroxy-L-arginine. The substrate-induced red shift correlates with hydrogen bonding between substrate and heme-bound oxygen resulting in conversion to a ferric heme-superoxy species
-
-
?
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3-bromo-7-nitroindazole
-
3-[2,4-di(6-amino-4-methylpyridin-2-yl)ethyl]benzonitrile
inhibitor binds to heme propionate A through a bifurcated H-bond and a pi-pi stacking interaction between the conserved Tyr and aminopyridine group
4-methylquinolin-2-amine
among the most potent aminoquinoline inhibitors tested, KS value 0.00080 mM
6,6'-[(5-amino-1,3-phenylene)di(ethane-2,1-diyl)]bis(4-methylpyridin-2-amine)
compound interacts with the active site Glu243 and heme propionate D through a series of hydrogen bonds between the aminopyridine functional groups. Comparison with inhibition of mammalian NOS isoforms
6,6'-[[(2S,3S)-2-aminobutane-1,3-diyl]bis(oxymethanediyl)]bis(4-methylpyridin-2-amine)
compound impedes the growth of Bacillus subtilis under oxidative stress an is able to displace the tetrahydrobiopterin cofactor in the Bacillus subtilis enzyme but not in the mouse enzyme
6,6'-[[5-(aminomethyl)-1,3-phenylene]di(ethane-2,1-diyl)]bis(4-methylpyridin-2-amine)
compound interacts with the active site Glu243 and heme propionate D through a series of hydrogen bonds between the aminopyridine functional groups. Comparison with inhibition of mammalian NOS isoforms
6-([(3R,5S)-5-][[[[(6-amino-4-methylpyridin-2-yl)methoxy]methyl]pyrrolidin-3-yl]oxy]methyl)-4-methylpyridin-2-amine
compound impedes the growth of Bacillus subtilis under oxidative stress
6-[5-([4-[(6-amino-4-methylpyridin-2-yl)methyl]pyrrolidin-3-yl]oxy)pentyl]-4-methylpyridin-2-amine
binding is stabilized by a 3.2 A H-bond between the pyrrolidine ring and the carbonyl group of tetrahydrobiopterin
N,N'-[[(2S)-3-aminopropane-1,2-diyl]bis(oxymethylene-3,1-phenylene)]di(thiophene-2-carboximidamide)
inhibitor binds by extending outside the active site to interact with a surface adjacent to residue Y357
N-omega-nitro-L-arginine
-
N1-[6-[2-(6-amino-4-methylpyridin-2-yl)ethyl]pyridin-2-yl]-N1,N2-dimethylethane-1,2-diamine
inhibitor binding distorts the pterin binding site by inducing an alternative rotameric position in residue W329. KS value 18.3 microM
-
Ngamma-nitro-L-arginine
-
competitive
quinolin-2-amine
among the most potent aminoquinoline inhibitors tested, KS value 0.00125 mM
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binding of substrate L-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthase from a loose dimer, with an exposed active center and higher sensitivity to proteolysis, to a tight dimer competent for catalysis
in complex with a number of inhibitors
in complex with cofactor tetrahydrofolate and substrate L-arginine or the intermediate Nomega-hydroxy-L-arginine to 1.9 or 2.2 Å resolution, respectively
in complex with inhibitors that target both the active and pterin sites
incomplex with inhibitors 6-([(3R,5S)-5-][[[[(6-amino-4-methylpyridin-2-yl)methoxy]methyl]pyrrolidin-3-yl]oxy]methyl)-4-methylpyridin-2-amine and 6,6'-[[(2S,3S)-2-aminobutane-1,3-diyl]bis(oxymethanediyl)]bis(4-methylpyridin-2-amine)
structures of the Fe(III)-NO complex with Nomega-hydroxy-L-arginine show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound Nomega-hydroxy-L-arginine. In the Fe(II)-NO complexes, the protonated Nomega-hydroxy-L-arginine Nomega atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. The L-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen
wild-tye and mutant I208V, in complex with inhibitors
wild-type in complex with inhibitors N-omega-nitro-L-arginine and 3-bromo-7-nitroindazole
to 3.2 A resolution. Residue Lys-356 (Bacillus subtilis NOS) is changed to Arg-365 (gsNOS), substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme
enzyme exhibits two conformations in the absence of substrate. The addition of L-Arg stabilizes the conformer more similar to the Mus muculus enzyme, whereas N-hydroxy-L-arginine stabilizes the conformer more similar to the Bacillus subtilis enzyme, although both substrates introduce a positive electrostatic potential to the distal heme pocket
-
to 2.4 A resolution. Heme and inhibitor S-ethylisothiourea are bound at the active site, while the intersubunit site has NAD+ bound. Enzyme is a dimer, with NAD+ in the interface ligand binding site. Heme is buried in the interior of each monomer
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E25A/E26A/E316A
mutant facilitates crystallization
E25A/E26A/E316A/Y357F
mutant facilitates crystallization
I208V
crystallization and inhibition data
P332G
mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type
P332G/A333S
mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme
W66L
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
W66Y
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
E25A/E26A/E316A
-
mutant facilitates crystallization
-
E25A/E26A/E316A/Y357F
-
mutant facilitates crystallization
-
I208V
-
crystallization and inhibition data
-
P332G
-
mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type
-
P332G/A333S
-
mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme
-
W66F
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66H
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66L
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66Y
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
L356R
mutation Lys-356 (Bacillus subtilis NOS) to Arg-365 (gsNOS) substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme
W66F
-
mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate
W66F
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
W66H
-
mutation changes midpoint potential from -361 mV for wild-type to -302 mV. Activity is similar to wild-type
W66H
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
additional information
a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity
additional information
the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions
additional information
-
the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions
-
additional information
-
a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity
-
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Wang, Z.; Lawson, R.J.; Buddha, M.R.; Wei, C.; Crane, B.R.; Munro, A.W.; Stuehr, D.J.
Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase
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Bacterial nitric-oxide synthases operate without a dedicated redox partner
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Bacillus anthracis, Bacillus subtilis
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Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase
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279
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2004
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286
39224-39235
2011
Bacillus subtilis
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NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum
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Sorangium cellulosum
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Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus
Structure
10
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Staphylococcus aureus (P0A004), Staphylococcus aureus
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Structure of a nitric oxide synthase heme protein from Bacillus subtilis
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41
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Bacillus subtilis (O34453), Bacillus subtilis 168 (O34453)
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Resonance Raman study of Bacillus subtilis NO synthase-like protein: Similarities and differences with mammalian NO synthases
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45
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Bacillus subtilis (O34453), Bacillus subtilis 168 (O34453)
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Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation
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Substrate-ligand interactions in Geobacillus stearothermophilus nitric oxide synthase
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47
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Inhibitor bound crystal structures of bacterial nitric oxide synthase
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54
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Bacillus subtilis (O34453), Bacillus subtilis 168 (O34453)
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