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Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

http://www.wikidata.org/entity/Q33923728

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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 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.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.Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Pulsed electron paramagnetic resonance study of domain docking in neuronal nitric oxide synthase: the calmodulin and output state perspective.Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins 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.Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase.Mutation in the flavin mononucleotide domain modulates magnetic circular dichroism spectra of the iNOS ferric cyano complex in a substrate-specific manner.Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling.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.Pulsed ENDOR determination of the arginine location in the ferrous-NO form of neuronal NOS.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.Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.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.Regulation 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.Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant.Dynamic control of electron transfers in diflavin reductases.Elucidating nitric oxide synthase domain interactions by molecular dynamics.Calmodulin-induced structural changes in endothelial nitric oxide synthase.Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.Calmodulin activates neuronal nitric oxide synthase by enabling transitions between conformational states.

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Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

http://www.wikidata.org/entity/Q33923728

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2009年の論文

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2009年論文

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2009年論文

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Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

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Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

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Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

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Dennis J Stuehr

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Jay L Zweier

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Kulwant S Aulak

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Mahinda Gangoda

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Robielyn P Ilagan

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Sougata Sinha Ray

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Zhi-Qiang Wang

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P2860

Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation

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

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes

Structure of a cytochrome P450-redox partner electron-transfer complex

N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization.

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

The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase

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