Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins. - Wikidata - awgldk - TriplyDB

Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.

Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.

http://www.wikidata.org/entity/Q36744200

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Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450 A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme Regulation of interdomain electron transfer in the NOS output state for NO production Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase.Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin Structural 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 synthase Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins Molecular architecture of mammalian nitric oxide synthases.Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Lobe-specific calcium binding in calmodulin regulates endothelial nitric oxide synthase activation.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.A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics study Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.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 complex Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of inducible nitric oxide synthase.Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.Gaseous neurotransmitters and their role in anapyrexia.Research progress on neurobiology of neuronal nitric oxide synthase.Dynamic control of electron transfers in diflavin reductases.Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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P2860

Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.

http://www.wikidata.org/entity/Q36744200

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2008 nî lūn-bûn

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... -oxide synthase flavoproteins.

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Differences in a conformationa ...... c-oxide synthase flavoproteins

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David W Konas

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Deborah Durra

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Dennis J Stuehr

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Mauro Tiso

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Robielyn P Ilagan

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Russ Hille

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P2860

Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution

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

Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase

A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies

NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer

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

Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation

Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes

Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase

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