ArticleThe Journal of biological chemistry2010
Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Immunomodulatory and anti-inflammatory potential of S-nitrosoglutathione (GSNO) in multiple sclerosis: a review of mechanisms and therapeutic perspectives.Frontiers in immunology · 2026Review
- In Silico and In Vitro Approach for Evaluation of the Anti-Inflammatory and Antioxidant Potential of Mygalin.International journal of molecular sciences · 2023Article
- Voltage-gated potassium channel proteins and stereoselective S-nitroso-l-cysteine signaling.JCI insight · 2020Article
- An Update on Thiol Signaling: S-Nitrosothiols, Hydrogen Sulfide and a Putative Role for Thionitrous Acid.Antioxidants (Basel, Switzerland) · 2020Review
- From Genetics to Precision Therapy: Finding a Path through the Scientific Valley of Death.American journal of respiratory cell and molecular biology · 2019Article
- Cyclic compression increases F508 Del CFTR expression in ciliated human airway epithelium.American journal of physiology. Lung cellular and molecular physiology · 2019Article
- PDI-mediated S-nitrosylation of DRP1 facilitates DRP1-S616 phosphorylation and mitochondrial fission in CA1 neurons.Cell death & disease · 2018Article
- Computational Structural Biology ofFrontiers in oncology · 2018Review
- A substrate trapping approach identifies proteins regulated by reversible S-nitrosylation.Molecular & cellular proteomics : MCP · 2014Article
- Fourier transform infrared spectroscopy study of ligand photodissociation and migration in inducible nitric oxide synthase.F1000Research · 2014Article
- Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling.Current opinion in chemical biology · 2012Review
- S-Nitrosylation signaling regulates cellular protein interactions.Biochimica et biophysica acta · 2012Review
- Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.Biochimica et biophysica acta · 2012Review
- Mechanism and kinetics of inducible nitric oxide synthase auto-S-nitrosation and inactivation.Biochemistry · 2012Article
- Membrane transfer of S-nitrosothiols.Nitric oxide : biology and chemistry · 2011Article
- All stressed out without ATM kinase.Science signaling · 2011Article
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Authors and funding
8 authors.
Funding
Abstract
Inducible nitric-oxide synthase (iNOS) produces biologically stressful levels of nitric oxide (NO) as a potent mediator of cellular cytotoxicity or signaling. Yet, how this nitrosative stress affects iNOS function in vivo is poorly understood. Here we define two specific non-heme iNOS nitrosation sites discovered by combining UV-visible spectroscopy, chemiluminescence, mass spectrometry, and x-ray crystallography. We detected auto-S-nitrosylation during enzymatic turnover by using chemiluminescence. Selective S-nitrosylation of the ZnS(4) site, which bridges the dimer interface, promoted a dimer-destabilizing order-to-disorder transition. The nitrosated iNOS crystal structure revealed an unexpected N-NO modification on the pterin cofactor. Furthermore, the structurally defined N-NO moiety is solvent-exposed and available to transfer NO to a partner. We investigated glutathione (GSH) as a potential transnitrosation partner because the intracellular GSH concentration is high and NOS can form S-nitrosoglutathione. Our computational results predicted a GSH binding site adjacent to the N-NO-pterin. Moreover, we detected GSH binding to iNOS with saturation transfer difference NMR spectroscopy. Collectively, these observations resolve previous paradoxes regarding this uncommon pterin cofactor in NOS and suggest means for regulating iNOS activity via N-NO-pterin and S-NO-Cys modifications. The iNOS self-nitrosation characterized here appears appropriate to help control NO production in response to cellular conditions.
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