Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation
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Tyrosine nitration is an oxidative post-translational modification that can occur in proteins associated to hydrophobic bio-structures such as membranes and lipoproteins. In this work, we have studied tyrosine nitration in membranes using a model system consisting of phosphatidylcholine liposomes with pre-incorporated tyrosine-containing 23 amino acid transmembrane peptides. Tyrosine residues were located at positions 4, 8 or 12 of the amino terminal, resulting in different depths in the bilayer. Tyrosine nitration was accomplished by exposure to peroxynitrite and a peroxyl radical donor or hemin in the presence of nitrite. In egg yolk phosphatidylcholine liposomes, nitration was highest for the peptide with tyrosine at position 8 and dramatically increased as a function of oxygen levels. Molecular dynamics studies support that the proximity of the tyrosine phenolic ring to the linoleic acid peroxyl radicals contributes to the efficiency of tyrosine oxidation. In turn, α-tocopherol inhibited both lipid peroxidation and tyrosine nitration. The mechanism of tyrosine nitration involves a "connecting reaction" by which lipid peroxyl radicals oxidize tyrosine to tyrosyl radical and was fully recapitulated by computer-assisted kinetic simulations. Altogether, this work underscores unique characteristics of the tyrosine oxidation and nitration process in lipid-rich milieu that is fueled via the lipid peroxidation process.
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Peroxynitrite can abstract a hydrogen atom to initiate lipid peroxidation, a detrimental process that can lead to cytotoxicity.
“For example, lipids are also a significant biological target for peroxynitrite, and although the species can abstract a hydrogen atom to initiate lipid peroxidation, a detrimental process that can lead to cytotoxicity in many cases (65, 766), peroxynitrite can also mediate lipid nitration (54, 1027).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [65]
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- Authors
- Bartesaghi, S., Herrera, D., Martinez, D. M., Petruk, A., Demicheli, V., Trujillo, M., Martí, M. A., Estrín, D. A., & Radi, R.
- Affiliations
- Universidad de la República de Uruguay (UY)
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- Corresponding author
- Bartesaghi, Silvina
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2017-05
- Volume
- 622
- Pages
- 9-25
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2606205906
- Cited by
- 18
- References
- 107
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 3 · 2018: 4 · 2017: 1
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Conicet (submittedVersion, cc-by-nc-sa)
- Funders
- Agencia Nacional de Investigación e Innovación (Fondo Clemente Estable (6605)
- Universidad de la República
- National Institutes of Health (AI095173)
- Fundación Manuel Pérez, Facultad de Medicina, Universidad de la República, Uruguay
- CNPq (203400/2014-3)
- International Centre of Genetic Engineering and Biotechnology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- tyrosine nitration, tyrosine oxidation, transmembrane peptides, lipid peroxidation, peroxy radicals, peroxynitrite, hemin, alpha-tocopherol, phosphatidylcholine liposomes, membrane proteins, post-translational modification, linoleic acid, tyrosyl radical, oxygen dependence, kinetic simulation
- MeSH terms
- Amidines, Amino Acid Sequence, Cell Membrane, Free Radicals, Hemin, Liposomes, Oxidation-Reduction, Oxygen, Peptides, Tyrosine, Lipid Peroxidation, Peroxynitrous Acid, Molecular Dynamics Simulation
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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