Cytochrome c Nitration by Peroxynitrite
Open accessAbstract
Peroxynitrite (ONOO(-)), the product of superoxide (O(2)) and nitric oxide (.NO) reaction, inhibits mitochondrial respiration and can stimulate apoptosis. Cytochrome c, a mediator of these two aspects of mitochondrial function, thus represents an important potential target of ONOO(-) during conditions involving accelerated rates of oxygen radical and.NO generation. Horse heart cytochrome c(3+) was nitrated by ONOO(-), as indicated by spectral changes, Western blot analysis, and mass spectrometry. A dose-dependent loss of cytochrome c(3+) 695 nm absorption occurred, inferring that nitration of a critical heme-vicinal tyrosine (Tyr-67) promoted a conformational change, displacing the Met-80 heme ligand. Nitration was confirmed by cross-reactivity with a specific antibody against 3-nitrotyrosine and by increased molecular mass compatible with the addition of a nitro-(-NO(2)) group. Mass analysis of tryptic digests indicated the preferential nitration of Tyr-67 among the four conserved tyrosine residues in cytochrome c. Cytochrome c(3+) was more extensively nitrated than cytochrome c(2+) because of the preferential oxidation of the reduced heme by ONOO(-). Similar protein nitration patterns were obtained by ONOO(-) reaction in the presence of carbon dioxide, whereupon secondary nitrating species arise from the decomposition of the nitroso-peroxocarboxylate (ONOOCO(2)(-)) intermediate. Peroxynitrite-nitrated cytochrome c displayed significant changes in redox properties, including (a) increased peroxidatic activity, (b) resistance to reduction by ascorbate, and (c) impaired support of state 4-dependent respiration in intact rat heart mitochondria. These results indicate that cytochrome c nitration may represent both oxidative and signaling events occurring during .NO- and ONOO(-)-mediated cell injury.
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Protein nitration can also occur through the reaction of nitrite with heme proteins in the presence of hydrogen peroxide.
“Importantly, protein nitration can also occur through the reaction of nitrite with heme proteins in the presence of hydrogen peroxide (153, 154).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [153]
The heme iron of cytochrome c is predominately hexacoordinate, but can become pentacoordinate when the iron-methionine bond is ruptured which occurs when the methionine is oxidized, tyrosines are nitrated, or the cytochrome interacts with anionic phospholipids.
“Similar to Ngb, the heme iron of cytochrome c is predominately hexacoordinate, but can become pentacoordinate when the iron-methionine bond is ruptured which occurs when the methionine is oxidized [65, 66], tyrosines are nitrated [67, 68], or the cytochrome interacts with anionic phospholipids such as those present in the inner membrane of the mitochondria [69–71].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [68]
In cytochrome c, transition from hexa- to pentacoordination is induced by Met-80 oxidation, Tyr-67 nitration, and interaction with anionic lipids such as cardiolipin.
“In the case of cytochrome c, transition from hexa- to pentacoordination has been shown to be induced by Met-80 oxidation [77], Tyr-67 nitration [78] and by interaction with anionic lipids such as cardiolipin [79].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [78]
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Nitric Oxide and Peroxynitrite in Health and Disease
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“This alternative protein (un)folding and disruption of the Fe–S(Met80) bond inevitably leads to an enhancement of peroxidase activity, similar to that caused by chemical modifications, such as carboxymethylation [49] and interactions with peroxynitrite [50] or hypochlorite [51], or complete unfolding in the presence o…”
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“This is useful for separative strategies based on isoelectric focusing of nitrated proteins (214, 215).”
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“Furthermore, within individual proteins, such as cytochrome c and RNAse certain tyrosine residues are more readily nitrated than others (Souza et al., 1999; Cassina et al., 2000).”
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“may indicate a protective role of the enzyme in its nonnitrated form. In addition, nitrated cytochrome c is also found in the cytosol [”
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“These residues, Tyr48 (highly conserved in eukaryotes), Tyr67, Tyr74 (conserved in many eukaryotes), Lys72 and Tyr97, are post-translationally regulated.”
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“to have profound effects on its redox-regulating properties (Cassina et al., 2000).”
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“Notably, nitration of cytochrome c upregulates its peroxidatic activity, which increases the production of hydrogen peroxide causing more oxidative damage to mitochondria [252,253].”
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Elevated retinal zeaxanthin and prevention of light-induced photoreceptor cell death in quail.
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“It is associated with the inner mitochondrial membrane through its interactions with cytochrome c1 and subunit II of cytochrome c oxidase and is found in relatively high concentration (approximately 400 M) in mitochondria [3–9].”
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“As another mechanism, ONOO– might modify the Bcl-2 family and change the localization and function, as in the case of Bax (35).”
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“peroxidase activity) (Batthyany et al., 2005; Cassina et al., 2000), protein kinase Ce (i.”
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“For example, nitration of cytochrome c yields a more acidic protein species with peroxidatic activity, leading to increased production of hydrogen peroxide and oxidation of membrane phospholipids in the mitochondrial membrane (Cassina et al. 2000).”
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Self-citationProtein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity
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“Cytochrome c Electron transfer and apoptosis Higher peroxidatic activity [74, 75] Decreased apoptosome activation [78] Fibrinogen Coagulation Higher aggregation [76] Protein kinase Cε Serine/threonine kinase Translocation and activation [77] α-Synuclein Presynaptic protein Higher aggregation [79] Nerve growth factor N…”
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Mitochondrial protein tyrosine nitration
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“tion disrupts the M80-Fe ligation of cyt c (5, 6, 21), and endogenous nitration of cyt c has been detected in vivo under conditions of nitrative stress (3, 4).”
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“[28] A.”
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“It has been demonstrated that oxidative or nitrative chemical modifications of the protein lead to the induction of significant peroxidase activity [17-19].”
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- Authors
- Cassina, A. M., Hodara, R., Souza, J. M., Thomson, L., Castro, L., Ischiropoulos, H., Freeman, B. A., & Radi, R.
- Affiliations
- Universidad de la República de Uruguay (UY)
- Children's Hospital of Philadelphia (US)
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 275
- Issue
- 28
- Pages
- 21409-21415
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2009279488
- Cited by
- 354
- References
- 57
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 4 · 2023: 7 · 2022: 2 · 2021: 6 · 2020: 7 · 2019: 5 · 2018: 8 · 2017: 9 · 2016: 5 · 2015: 5 · 2014: 17 · 2013: 9 · 2012: 22
- FWCI
- 7.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG 13966, R01AG013966)
- National Heart, Lung, and Blood Institute (HL54926, R01HL054926)
- Fogarty International Center (R03-TW0099)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- cytochrome c, peroxynitrite, nitration, nitrotyrosine, mitochondrial respiration, apoptosis, nitric oxide, superoxide, redox properties, heart mitochondria, oxidative stress
- MeSH terms
- Animals, Binding Sites, Cytochrome c Group, Horses, Kinetics, Mitochondria, Heart, Models, Molecular, Molecular Conformation, Nitrates, Peptide Mapping, Protein Conformation, Spectrophotometry, Mass Spectrometry, Trypsin, Oxidants, Rats
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