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(6R)-5,6,7,8-tetrahydro-L-biopterin
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2',3'-dialdehyde analogue of NADPH
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activation, can substitute for NADPH at low concentrations, inhibitory at concentrations of 40times the apparent Km-value or after prolonged incubation
2,6-dichlorophenolindophenol
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activation
5,6,7,8-tetrahydro-L-biopterin
flavodoxin
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reduced YkuN and YkuP containing FMN, YkuN is more efficient in supporting bsNOS catalysis, Km for YkuN is 0.0016 mM, for YkuP 0.022 mM, overview
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flavodoxin I
binding site sequence, overview
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NADP+
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binding mechanism
nitroblue tetrazolium
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activation
(6R)-tetrahydrobiopterin
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-
(6R)-tetrahydrobiopterin
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(6R)-tetrahydrobiopterin
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required
(6R)-tetrahydrobiopterin
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enzyme-bound
5,6,7,8-tetrahydro-L-biopterin
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-
5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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5,6,7,8-tetrahydro-L-biopterin
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-
5,6,7,8-tetrahydro-L-biopterin
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stimulates
5,6,7,8-tetrahydro-L-biopterin
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required
5,6,7,8-tetrahydro-L-biopterin
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required
5,6,7,8-tetrahydro-L-biopterin
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required
5,6,7,8-tetrahydro-L-biopterin
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required
5,6,7,8-tetrahydro-L-biopterin
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enzyme purified in absence of biopterin contains substoichiometric concentration, if purified in presence of biopterin it contains 1 mol biopterin per mol MW 130000 subunit
5,6,7,8-tetrahydro-L-biopterin
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presumably tightly enzyme-bound
5,6,7,8-tetrahydro-L-biopterin
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0.19 mol bound per mol of dimer
5,6,7,8-tetrahydro-L-biopterin
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stimulates 9fold
5,6,7,8-tetrahydro-L-biopterin
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absolute requirement, recombinant from Pichia pastoris
5,6,7,8-tetrahydro-L-biopterin
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enhances initial rate of NO-formation
5,6,7,8-tetrahydro-L-biopterin
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activity is correlated directly to bound biopterin concentration
5,6,7,8-tetrahydro-L-biopterin
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not required for activity
5,6,7,8-tetrahydro-L-biopterin
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required for the first partial reaction, formation of NG-hydroxy-L-arginine
5,6,7,8-tetrahydro-L-biopterin
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i.e. (6R)-2-amino-4-hydroxy-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridine, 6R-isomer, requirement, biopteroflavoprotein, 1 mol tetrahydrobiopterin per mol enzyme dimer
5,6,7,8-tetrahydro-L-biopterin
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stimulates 4fold at 0.001 mM
5,6,7,8-tetrahydro-L-biopterin
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0.04 mol per mol of subunit
5,6,7,8-tetrahydro-L-biopterin
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only wild-type
5,6,7,8-tetrahydro-L-biopterin
0.003 mM
Calmodulin
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Calmodulin
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dependent on
Calmodulin
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murine macrophage enzyme is Ca2+/calmodulin independent
Calmodulin
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the enzyme bears a Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
Calmodulin
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rat neutrophil enzyme is calmodulin independent
Calmodulin
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activation, potent stimulator of purified, not crude, enzyme preparation
Calmodulin
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Ca2+/calmodulin is required for superoxide formation in absence of tetrahydropterin
Calmodulin
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Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
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Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
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enzyme-bound is required, supplemented stimulates
Calmodulin
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dependent on, endothelial enzyme
Calmodulin
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dependent on, endothelial enzyme
Calmodulin
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no stimulation with exogenous calmodulin, inducible isoform from liver
Calmodulin
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15fold stimulation of cytochrome c reduction of wild-type and mutants C415A and C415H
Calmodulin
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NADPH-diaphorase activity of the enzyme is Ca2+/calmodulin independent
Calmodulin
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enzyme-bound, the binding sequence links the two enzyme domains
Calmodulin
in the absence of calmodulin, the wild type enzyme activity is less than 15% of the maximum calmodulin-dependent values
Calmodulin
maximum calmodulin-dependent activity is measured at 1.5 mM CaCl2, phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca2+ concentrations required for calmodulin to bind and activate the enzyme
cytochrome c
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cytochrome c
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activation
FAD
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FAD
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tightly enzyme-bound
FAD
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2.2 mol FAD per mol of enzyme dimer
FAD
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1 mol FAD per mol enzyme dimer
FAD
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the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
FAD
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wild-type and mutant C415H contain1 mol per mol of subunit
FAD
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1 mol per mol of enzyme subunit
FAD
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non-covalently bound FAD
FAD
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FAD containing flavoprotein
FAD
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FAD containing flavoprotein
FAD
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0.56 mol per mol of recombinant enzyme
FAD
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absolute requirement for FAD
FAD
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major source of superoxide production in absence of tetrahydrobiopterin
FAD
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slight activation by exogeneous FAD
FAD
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no activation by the addition of exogenous FAD
FAD
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0.49 mol per mol of dimer
FAD
binding site sequence, overview
FAD
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required for catalysis
FAD
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electron flow within the neuronal nitric oxide synthase reductase domain includes hydride transfer from NADPH to FAD followed by two one-electron transfer reactions from FAD to FMN. Binding of the second NADPH is necessary to drive the full reduction of FMN and charge transfer and the subsequent interflavin electron transfer have distinct spectral features that can be monitored separately with stopped flow spectroscopy. Interflavin electron transfer reported at 600 nm is not limiting in nitric oxide synthase catalysis
FAD
during catalysis, NADPH-derived electrons are transfered into FAD and then distributed into the FMN domain for further transfer to internal or external heme groups. Conformational freedom of the FMN domain is essential for the electron transfer
FAD
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation
FMN
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FMN
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tightly enzyme-bound
FMN
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the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
FMN
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1 mol per mol of enzyme subunit
FMN
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wild-type and mutant C415H contain 0.8 and 0.9 mol per mol of subunit, respectively
FMN
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1 mol FMN per mol enzyme dimer
FMN
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no activation by the addition of exogenous FMN
FMN
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1.1 mol FMN per mol enzyme dimer
FMN
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FMN containing flavoprotein
FMN
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FMN containing flavoprotein
FMN
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0.79 mol per mol of recombinant enzyme
FMN
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0.71 mol per mol of dimer
FMN
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FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
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an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
FMN
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regulation of the FMN module conformational equilibrium, overview
FMN
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required for catalysis
FMN
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determination of FMN-heme intraprotein electron transfer kinetics in full length and oxygenase/FMN construct of human inducible nitric oxide synthase. The rate constant increases considerably with temperature. The FMN domain in the holoenzyme needs to sample more conformations before the intraprotein electron transfer takes place, and the FMN domain in the oxyFMN construct is better poised for efficient intraprotein electron transfer
FMN
during catalysis, NADPH-derived electrons are transfer into FAD and then distributed into the FMN domain for further transfer to internal or external heme groups. Conformational freedom of the FMN domain is essential for the electron transfer
FMN
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation
FMN
proposed conformational model for nitric oxide synthesis by the enzyme. Nitric oxide synthesis involves two distinct changes in the holoenzyme complex: 1. an extended-to-closed conformational equilibrium that brings the reductase domains together in a cross-monomer arrangement, and 2. release and rotation of the FMN domain triggered by CaM binding that positions the FMN cofactor for electron transfer across to the adjacent oxygenase domain in the closed state
heme
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heme
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an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
heme
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frequencies of electron transfer, overview
heme
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frequencies of electron transfer, overview
heme
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the heme is coordinated by a cysteine residue on the proximal side, and the substrates, Arg or N-hydroxy-L-arginine, bind above the heme iron atom in the distal pocket, while the cofactor, tetrahydrobiopterin, binds along the side of the heme
heme b
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bound, quantitative determination
heme b
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bound, quantitative determination
NADPH
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NADPH
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440192, 440193, 440195, 440198, 440200, 440201, 440206, 440209, 440217, 440221, 440222, 440225, 440234, 440236, 440238, 440239, 672016, 673662, 674558, 684317, 686293, 687548, 687727, 688600, 696643
NADPH
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440190, 440191, 440192, 440198, 440203, 440208, 440213, 440220, 440228, 440230, 440236, 658119, 659257, 659330, 671278, 671728, 672363, 672524, 675257, 686293, 687615, 699997
NADPH
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requirement, specific for, NADPH-diaphorase activity requires higher NADPH concentrations than nitric oxide formation
NADPH
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at high concentration inhibits dimer reconstitution from subunits
NADPH
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NADPH-dependent dioxygenase
NADPH
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NADPH-dependent dioxygenase
NADPH
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crude preparation requires only NADPH as cofactor
NADPH
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binding mechanism
NADPH
binding site sequence, overview
NADPH
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binding structure of NADP(H) to wild-type and truncation mutant enzyme lacking parts of the C-terminus, overview
NADPH
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required for catalysis
NADPH
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electron flow within the neuronal nitric oxide synthase reductase domain includes hydride transfer from NADPH to FAD followed by two one-electron transfer reactions from FAD to FMN. Binding of the second NADPH is necessary to drive the full reduction of FMN and charge transfer and the subsequent interflavin electron transfer have distinct spectral features that can be monitored separately with stopped flow spectroscopy. Interflavin electron transfer reported at 600 nm is not limiting in nitric oxide synthase catalysis
NADPH
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry
NADPH
provided from the nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH diaphorase) activity. In the brain, NADPH diaphorase (NADPH-d) and nNOS are strictly co-localized
tetrahydrobiopterin
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tetrahydrobiopterin
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required
tetrahydrobiopterin
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oxidation product of BH4 is a protonated BH3 radical, key role of BH4 in protonation of Fe(II)-O2-, overview
tetrahydrobiopterin
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oxidation product of BH4 is a protonated BH3 radical, key role of BH4 in protonation of Fe(II)-O2-, overview
tetrahydrobiopterin
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binding analysis
tetrahydrobiopterin
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the cofactor tetrahydrobiopterin binds along the side of the heme