Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis. - Wikidata - awgldk - TriplyDB

Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.

Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.

http://www.wikidata.org/entity/Q37156500

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Signaling and stress: The redox landscape in NOS2 biology Dissecting structural and electronic effects in inducible nitric oxide synthase Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Towards the free energy landscape for catalysis in mammalian nitric oxide synthases.Energy landscapes and catalysis in nitric-oxide synthase.Nanodiscs in Membrane Biochemistry and Biophysics.A perspective on conformational control of electron transfer in nitric oxide synthases.The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.

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P2860

Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.

http://www.wikidata.org/entity/Q37156500

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 July 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Thermodynamic characterization ...... tric oxide synthase catalysis.

@en

Thermodynamic characterization ...... tric oxide synthase catalysis.

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type

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Thermodynamic characterization ...... tric oxide synthase catalysis.

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Thermodynamic characterization ...... tric oxide synthase catalysis.

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Thermodynamic characterization ...... tric oxide synthase catalysis.

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Thermodynamic characterization ...... tric oxide synthase catalysis.

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Thermodynamic characterization ...... itric oxide synthase catalysis

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Dennis J Stuehr

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Mekki Bayachou

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Mohammad Mahfuzul Haque

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Mohammed Fadlalla

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Zhi-Qiang Wang

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P2860

Nitric oxide synthases in mammals

Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase

Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation

Structure of nitric oxide synthase oxygenase dimer with pterin and substrate

Nitric oxide synthases: structure, function and inhibition

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Protein control of true, gated, and coupled electron transfer reactions.

Mechanistic studies on the reversible binding of nitric oxide to metmyoglobin.

Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase.

Substrate binding favors enhanced NO binding to P450cam.

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4439-4453

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scholarly article

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10.1111/FEBS.12404

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