The FAD-shielding residue Phe1395 regulates neuronal nitric-oxide synthase catalysis by controlling NADP+ affinity and a conformational equilibrium within the flavoprotein domain.
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A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanismCorrelating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic TrapNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.NO formation by neuronal NO-synthase can be controlled by ultrafast electron injection from a nanotrigger.Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transferStructural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthaseSurface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.A connecting hinge represses the activity of endothelial nitric oxide synthase.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complexCharge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.Catalytic reduction of a tetrahydrobiopterin radical within nitric-oxide synthase.Exploring the electron transfer properties of neuronal nitric-oxide synthase by reversal of the FMN redox potential.A perspective on conformational control of electron transfer in nitric oxide synthases.Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.Dissecting the kinetics of the NADP(+)-FADH2 charge transfer complex and flavin semiquinones in neuronal nitric oxide synthase.Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.Inhibition of neuronal nitric-oxide synthase by phosphorylation at Threonine1296 in NG108-15 neuronal cells.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase.
P2860
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P2860
The FAD-shielding residue Phe1395 regulates neuronal nitric-oxide synthase catalysis by controlling NADP+ affinity and a conformational equilibrium within the flavoprotein domain.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@en
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@nl
type
label
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@en
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@nl
prefLabel
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@en
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@nl
P2093
P2860
P356
P1476
The FAD-shielding residue Phe1 ...... ithin the flavoprotein domain.
@en
P2093
David W Konas
Dennis J Stuehr
Gary W Brudvig
Kulwant S Aulak
Manisha Sharma
P2860
P304
35412-35425
P356
10.1074/JBC.M400872200
P407
P577
2004-06-04T00:00:00Z