Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase. - Wikidata - awgldk - TriplyDB

Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.

Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.

http://www.wikidata.org/entity/Q37438886

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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.Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase.Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics study Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Elucidating nitric oxide synthase domain interactions by molecular dynamics.A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.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.

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Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.

http://www.wikidata.org/entity/Q37438886

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2013

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Charge-pairing interactions co ...... euronal nitric oxide synthase.

@en

Charge-pairing interactions co ...... euronal nitric oxide synthase.

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type

label

Charge-pairing interactions co ...... euronal nitric oxide synthase.

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Charge-pairing interactions co ...... euronal nitric oxide synthase.

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Charge-pairing interactions co ...... euronal nitric oxide synthase.

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Charge-pairing interactions co ...... euronal nitric oxide synthase.

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Biochemical Journal

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Charge-pairing interactions co ...... euronal nitric oxide synthase.

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Deborah Durra

http://www.w3.org/2001/XMLSchema#string

Dennis J Stuehr

http://www.w3.org/2001/XMLSchema#string

Mekki Bayachou

http://www.w3.org/2001/XMLSchema#string

Mohammad Mahfuzul Haque

http://www.w3.org/2001/XMLSchema#string

Mohammed A Fadlalla

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P2860

Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation

Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1

Role of Asp1393 in catalysis, flavin reduction, NADP(H) binding, FAD thermodynamics, and regulation of the nNOS flavoprotein

Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase

Structure of nitric oxide synthase oxygenase dimer with pterin and substrate

Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation

The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.

Mammalian nitric oxide synthases.

Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer

Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.

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607-617

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scholarly article

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10.1042/BJ20121488

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P433

3

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450

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2013-03-01T00:00:00Z

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23289611

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3882132

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