Peroxynitrite Mediates Active Site Tyrosine Nitration in Manganese Superoxide Dismutase. Evidence of a Role for the Carbonate Radical Anion
Open accessAbstract
Protein tyrosine nitration has been observed in a variety of human diseases associated with oxidative stress, such as inflammatory, neurodegenerative, and cardiovascular conditions. However, the pathways leading to nitration of tyrosine residues are still unclear. Recent studies have shown that peroxynitrite (PN), produced by the reaction of superoxide and nitric oxide, can lead to protein nitration and inactivation. Tyrosine nitration may also be mediated by nitrogen dioxide produced by the oxidation of nitrite by peroxidases. Manganese superoxide dismutase (MnSOD), which plays a critical role in cellular defense against oxidative stress by decomposing superoxide within mitochondria, is nitrated and inactivated under pathological conditions. In this study, MnSOD is shown to catalyze PN-mediated self-nitration. Direct, spectroscopic observation of the kinetics of PN decay and nitrotyrosine formation (k(cat) = 9.3 × 10(2) M(-1) s(-1)) indicates that the mechanism involves redox cycling between Mn(2+) and Mn(3+), similar to that observed with superoxide. Distinctive patterns of tyrosine nitration within MnSOD by various reagents were revealed and quantified by MS/MS analysis of MnSOD trypsin digest peptides. These analyses showed that three of the seven tyrosine residues of MnSOD (Tyr34, Tyr9, and Tyr11) were the most susceptible to nitration and that the relative amounts of nitration of these residues varied widely depending upon the nature of the nitrating agent. Notably, nitration mediated by PN, in both the presence and absence of CO2, resulted in nitration of the active site tyrosine, Tyr34, while nitration by freely diffusing nitrogen dioxide led to surface nitration at Tyr9 and Tyr11. Flux analysis of the nitration of Tyr34 by PN-CO2 showed that the nitration rate coincided with the kinetics of the reaction of PN with CO2. These kinetics and the 20-fold increase in the efficiency of tyrosine nitration in the presence of CO2 suggest a specific role for the carbonate radical anion (•CO3(-)) in MnSOD nitration by PN. We also observed that the nitration of Tyr34 caused inactivation of the enzyme, while nitration of Tyr9 and Tyr11 did not interfere with the superoxide dismutase activity. The loss of MnSOD activity upon Tyr34 nitration implies that the responsible reagent in vivo is peroxynitrite, acting either directly or through the action of •CO3(-).
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eNOS has been shown to enter the mitochondrion of pulmonary smooth muscle cells upon stimulation with asymmetric dimethyl arginine or endothelin-1.
“For example, eNOS has been shown to enter the mitochondrion of pulmonary smooth muscle cells upon stimulation with asymmetric dimethyl arginine or endothelin-1 (768, 916).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [916]
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Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects
Batthyány, C., Bartesaghi, S., Mastrogiovanni, M., Lima, A., Demicheli, V., & Radi, R. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6787 · Cited by 86 · see citing works
Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214049 · Cited by 71 · see citing works
- Authors
- Surmeli, N. B., Litterman, N. K., Miller, A.-F., & Groves, J. T.
- Affiliations
- Department of Chemistry, Princeton University, Princeton New Jersey 08544, United States, and Department of Chemistry, University of Kentucky, Lexington, Kentucky 40506, United States
- University of Kentucky (US)
- Corresponding author
- Groves, John T.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-11-16
- Volume
- 132
- Issue
- 48
- Pages
- 17174-17185
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC3050995
- OpenAlex
- W2041443867
- Cited by
- 94
- References
- 97
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 6 · 2022: 5 · 2021: 2 · 2020: 4 · 2019: 7 · 2018: 9 · 2017: 4 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 15 · 2012: 9
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R37GM036298)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- ASE, manganese superoxide dismutase, peroxynitrite, tyrosine nitration, nitrotyrosine, carbonate radical anion, active site tyrosine, enzyme inactivation, redox cycling, nitric oxide, superoxide, oxidative stress, nitration kinetics, nitrite oxidation, peroxidase
- MeSH terms
- Azides, Carbon Dioxide, Carbonates, Escherichia coli, Free Radicals, Models, Molecular, Nitro Compounds, Superoxide Dismutase, Tyrosine, Catalytic Domain, Peroxynitrous Acid, Biocatalysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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