Rapid calmodulin-dependent interdomain electron transfer in neuronal nitric-oxide synthase measured by pulse radiolysis.
about
A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxificationStructural 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 synthaseThe Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function RelationshipsElectron supply and catalytic oxidation of nitrogen by cytochrome P450 and nitric oxide synthase.Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.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 complexMenaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase.Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock.Mechanistic studies on the intramolecular one-electron transfer between the two flavins in the human neuronal nitric-oxide synthase and inducible nitric-oxide synthase flavin domains.Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase.Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.
P2860
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P2860
Rapid calmodulin-dependent interdomain electron transfer in neuronal nitric-oxide synthase measured by pulse radiolysis.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@en
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@nl
type
label
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@en
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@nl
prefLabel
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@en
Rapid calmodulin-dependent int ...... measured by pulse radiolysis.
@nl
P2093
P2860
P356
P1476
Rapid calmodulin-dependent int ...... e measured by pulse radiolysis
@en
P2093
P2860
P304
39864-39871
P356
10.1074/JBC.M102537200
P407
P50
P577
2001-08-22T00:00:00Z