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Open AccessJournal ArticleDOI

The Ferrous-dioxy Complex of Neuronal Nitric Oxide Synthase: DIVERGENT EFFECTS OF l-ARGININE AND TETRAHYDROBIOPTERIN ON ITS STABILITY

TLDR
The spectral and kinetic properties of the intermediate identify it as the FeIIO2 complex of nNOSoxy, which may be important regarding the role of this cofactor in NO synthesis.
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This article is published in Journal of Biological Chemistry.The article was published on 1997-07-11 and is currently open access. It has received 149 citations till now. The article focuses on the topics: Tetrahydrobiopterin & Ferrous.

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Citations
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Journal ArticleDOI

Nitric oxide synthases: structure, function and inhibition

TL;DR: This review concentrates on advances in nitric oxide synthase (NOS) structure, function and inhibition made in the last seven years, during which time substantial advances have been made in the authors' understanding of this enzyme family.
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Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors

TL;DR: The mechanism of superoxide generation by endothelial nitric oxide synthase (eNOS) was investigated by the electron spin resonance spin-trapping technique using 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide as discussed by the authors.
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Mammalian nitric oxide synthases.

TL;DR: This report summarizes some of the current information regarding NO synthase structure-function, reaction mechanism, control of catalysis, and protein interactions.
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Enzymatic function of nitric oxide synthases.

TL;DR: The pteridine tetrahydrobiopterin (BH4) is a key feature of NOS, affecting dimerisation and electron transfer, although its full role in catalysis remains to be determined.
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Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.

TL;DR: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitricoxide.
References
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Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase.

TL;DR: Cloning of a complementary DNA for brain nitric oxide synthase reveals recognition sites for NADPH, FAD, flavin mononucleotide and calmodulin as well as phosphorylation sites, indicating that the synthase is regulated by many different factors.
Journal ArticleDOI

NO at work

Harald H.H.W. Schmidt, +1 more
- 23 Sep 1994 - 
TL;DR: NO is a double-edged sword, beneficial as a messenger or modulator and for immunologic self-defense, but potentially toxic in several different scenarios with factors such as oxidative stress, generation of reactive oxygen intermediates (ROls), and deficient anti- oxidant systems.
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