ArticleProceedings of the National Academy of Sciences of the United States of America2000
An autocatalytic mechanism of protein nitrosylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Biological activity of nitric oxide in the plasmatic compartment.Proceedings of the National Academy of Sciences of the United States of America · 2004Trial
- Identification of an Activity Selector for the Nitroso-Forming Activity in Bacterial Type-III Copper Enzymes.Angewandte Chemie (International ed. in English) · 2025Article
- Effects of Animal-Based and Plant-Based Nitrates and Nitrites on Human Health: Beyond Nitric Oxide Production.Biomolecules · 2025Review
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Pillars and Gaps of S-Nitrosylation-Dependent Epigenetic Regulation in Physiology and Cancer.Life (Basel, Switzerland) · 2021Review
- Beyond repression of Nrf2: An update on Keap1.Free radical biology & medicine · 2020Review
- Keap1 controls protein S-nitrosation and apoptosis-senescence switch in endothelial cells.Redox biology · 2020Article
- Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling.Antioxidants & redox signaling · 2019Review
- Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their RegulationPhysiological reviews · 2019Review
- Computational Structural Biology ofFrontiers in oncology · 2018Review
- Mechanism and catalytic strategy of the prokaryotic-specific GTP cyclohydrolase-IB.The Biochemical journal · 2017Article
- Postprandial lipids accelerate and redirect nitric oxide consumption in plasma.Nitric oxide : biology and chemistry · 2016Article
- Cytotoxic Potential of Bacillus cereus Strains ATCC 11778 and 14579 Against Human Lung Epithelial Cells Under Microaerobic Growth Conditions.Frontiers in microbiology · 2016Article
- Theoretical studies of the role of C-terminal cysteines in the process of S-nitrosylation of human Src kinases.Journal of molecular modeling · 2016Article
- Routes for formation of S-nitrosothiols in blood.Cell biochemistry and biophysics · 2013Review
- Redox signaling in cardiovascular health and disease.Free radical biology & medicine · 2013Review
- Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.Chemical reviews · 2013Review
- Nitric oxide-based protein modification: formation and site-specificity of protein S-nitrosylation.Frontiers in plant science · 2013Article
- The chemical biology of S-nitrosothiols.Antioxidants & redox signaling · 2012Review
- Redox regulation of mitochondrial function.Antioxidants & redox signaling · 2012Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitros(yl)ation is a widespread protein modification that occurs during many physiological and pathological processes. It can alter both the activity and function of a protein. Nitric oxide (( small middle dot)NO) has been implicated in this process, but its mechanism remained uncertain. ( small middle dot)NO is unable to react with nucleophiles under oxygen-free conditions, suggesting that its higher oxides, such as N(2)O(3), were actually nitrosylating agents. However, low concentrations and short lifespans of these species in vivo raise the question of how they could efficiently locate target proteins. Here we demonstrate that at physiological concentrations of ( small middle dot)NO, N(2)O(3) forms inside protein-hydrophobic cores and causes nitrosylation within the protein interior. This mechanism of protein modification has not been characterized, because all previously described mechanisms (e.g., phosphorylation, acetylation, ADP-ribosylation, etc.) occur via attack on a protein by an external modification agent. Oxidation of ( small middle dot)NO to N(2)O(3) is facilitated by micellar catalysis, which is mediated by the hydrophobic phase of proteins. Thus, a target protein seems to be a catalyst of its own nitrosylation. One of the applications of this finding, as we report here, is the design of specific hydrophobic compounds whose cooperation with ( small middle dot)NO and O(2) allows the rapid inactivation of target enzymes to occur.
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