Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail.
about
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.Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domainRegulation of interdomain electron transfer in the NOS output state for NO productionLys842 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.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.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.Intra- and inter-molecular effects of a conserved arginine residue of neuronal and inducible nitric oxide synthases on FMN and calmodulin binding.A mental retardation-linked nonsense mutation in cereblon is rescued by proteasome inhibition.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 complexRegulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase.Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.Dynamic control of electron transfers in diflavin reductases.Towards the free energy landscape for catalysis in mammalian nitric oxide synthases.Energy landscapes and catalysis in nitric-oxide synthase.A perspective on conformational control of electron transfer in nitric oxide synthases.Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.
P2860
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P2860
Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
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2007年學術文章
@zh-hant
name
Versatile regulation of neuron ...... egions of its C-terminal tail.
@en
Versatile regulation of neuron ...... egions of its C-terminal tail.
@nl
type
label
Versatile regulation of neuron ...... egions of its C-terminal tail.
@en
Versatile regulation of neuron ...... egions of its C-terminal tail.
@nl
prefLabel
Versatile regulation of neuron ...... egions of its C-terminal tail.
@en
Versatile regulation of neuron ...... egions of its C-terminal tail.
@nl
P2093
P356
P1433
P1476
Versatile regulation of neuron ...... regions of its C-terminal tail
@en
P2093
Dennis J Stuehr
Kulwant S Aulak
Mauro Tiso
P304
14418-14428
P356
10.1021/BI701646K
P407
P577
2007-11-20T00:00:00Z