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Journal ArticleDOI

A novel nonenzymatic pathway for the generation of nitric oxide by the reaction of hydrogen peroxide and D- or L-arginine.

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TLDR
A novel non-enzymatic pathway for NO synthesis involving hydrogen peroxide and D- or L-arginine and the addition of carboxy-2-phenyl-4, 4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxide (PTIO) is demonstrated, confirming NO generation in the reaction.
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 1997-04-07. It has received 166 citations till now. The article focuses on the topics: Hydrogen peroxide & Chemiluminescence.

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Citations
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The physiology and pathophysiology of nitric oxide in the brain.

TL;DR: Nitric oxide is a well-known vasorelaxant agent, but it works as a neurotransmitter when produced by neurons and is also involved in defense functions when it is produced by immune and glial cells.
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Role of nitric oxide in wound repair

TL;DR: What is known about the role of NO in wound healing and the exact mechanisms of action of NO on wound healing parameters are still unknown are summarized.
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Nitric oxide and nitric oxide synthase activity in plants

TL;DR: In plants, the enzymatic production of the signal molecule NO, either constitutive or induced by different biotic/abiotic stresses, may be a much more common event than was initially thought.
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Characterization of a Nitric Oxide Synthase from the Plant Kingdom: NO Generation from the Green Alga Ostreococcus tauri Is Light Irradiance and Growth Phase Dependent

TL;DR: This study characterizes a nitric oxide synthase (NOS) from Ostreococcus tauri, a marine green alga, and found the amino acid sequence of O. tauri NOS was found to be 45% similar to that of human NOS.

Molecules of Interest Nitric oxide and nitric oxide synthase activity in plants

TL;DR: In this paper, two genes of plant proteins with NOS activity have been isolated and characterized for the first time, and both proteins do not have sequence similarities to any mammalian NOS isoform.
References
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Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor

TL;DR: NO released from endothelial cells is indistinguishable from EDRF in terms of biological activity, stability, and susceptibility to an inhibitor and to a potentiator.
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Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide.

TL;DR: It is proposed that superoxide dismutase may protect vascular tissue stimulated to produce superoxide and NO under pathological conditions by preventing the formation of peroxynitrite.
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Vascular endothelial cells synthesize nitric oxide from L-arginine.

TL;DR: It is demonstrated that NO can be synthesized from L-arginine by porcine aortic endothelial cells in culture and the strict substrate specificity of this reaction suggests that L- arginine is the precursor for NO synthesis in vascular endothelium cells.
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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.
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