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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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“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]
In the citing paper
“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 the citing paper
“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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“4) at 20uC, followed by measuring the increase in absorbance at 420 nm [44].”
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“, 1995), while no significant tyrosine nitration was observed (Cassina et al., 2000).”
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“This nitration induces a conformation change, displacing methionine 80 residue and increasing the enzyme peroxidatic activity (Cassina et al., 2000).”
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Cardiovascular Redox and Ox Stress Proteomics
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“1 2-oxoglutarate dehydrogenase S-Nitrosylation (51) 2 3-oxoacid CoA transferase 1 Sulfenylation (46) 3 14 - 3–3 protein epsilon S-Nitrosylation C(192) (38) 4 14 - 3–3 protein eta S-Nitrosylation C(112) (38) 5 14 - 3–3 protein zeta/delta S-Nitrosylation C(94) (38) 6 Aconitase 2 S-Glutathionylation C(126),C(385) (86, 11…”
Perez, A. C., de Oliveira, A. C. C., Estévez, E., Molina, A. J., Prieto, J. G., & Álvarez, A. I. (2003) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/s1532-0456(02)00247-8 · Cited by 25
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“Nitrated cytochrome c has enhanced peroxidase activity, and as such can exacerbate oxidative injury (Cassina et al., 2000).”
BackgroundIs · NO News Bad News in Acute Respiratory Distress Syndrome?
Baldus, S. E., Castro, L., Eiserich, J. P., & Freeman, B. Α. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.163.2.ed2000c · Cited by 24
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“mediated injury of neuronal cells (Cassina et al., 2000).”
BackgroundInfluentialEffect of insulin nitration by peroxynitrite on its biological activity
Chi, Q., Wang, T., & Huang, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.034 · Cited by 24
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“…I (NADH ubiquinone reductase; Barker et al., 1996; Bolanos et al., 1996), complex II (succinate ubiquinone reductase), complex III (ubiquinol cytochrome c reductase), complex IV (cytochrome c oxidase) in the electron transport chain (Bolanos et al., 1995) and cytochrome c (Cassina et al., 2000).”
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“Under suitable conditions NO produces reactive nitrating species, peroxynitrite and nitrogen dioxide, which oxidize some tyrosine residues to generate 3-nitrotyrosine (Fig. 2). This important post-translational modification can have profound effects on protein function ranging from inactivation (85,86) to gain in func…”
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Oxidative Stress and Heart Failure
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“Previous work has shown that ONOO − is not likely to drive cyt c modifications under the experimental conditions used here, since SIN-1-treated cyt c does not exhibit the spectral characteristics of nitrated cyt c produced by direct reaction with ONOO − [18].”
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“For instance, nitration tryrosine groups of protein kinase-C e (Balafanova et al., 2002), fibrinogen (Vadseth et al., 2004), and cytochrome C (Cassina et al., 2000) result in aberrant gain of function.”
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“Additionally, the tyrosine nitration and inactivation of manganese superoxide dismutase (MnSOD) [9, 11] and cytochrome c [30, 31 ] by peroxynitrite can amplify mitochondrial injury and lead to pro-apoptotic signaling.”
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Covalent Modification of Cytochrome c Exposed to trans,trans-2,4-Decadienal
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Darley-Usmar, V. M., Patel, R. P., O’Donnell, V. B., & Freeman, B. Α. (2000) · Elsevier eBooks · doi:10.1016/b978-012370420-7/50018-6 · Cited by 21
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“Peroxynitrite promotes oxidative damage by reacting in complex ways with different biomolecules (Cassina et al., 2000), including the nitration of peptides and proteins, in the phenyl side chain of tyrosine residues, which may occur under physiological conditions, but levels have been found to…”
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Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation
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“…methodologies such as proteomics has revealed some specificity in protein site nitration and consequent modification or loss of function that is especially relevant if this mechanism involves enzymes of pathophysiological significance (Cassina et al 2000; Balafanova et al 2002; Vadseth et al 2004).”
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“or loss of function (Cassina et al., 2000; Nowak & Wachowicz, 2002; Szabo et al., 2007).”
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The kinetics of the reaction of nitrogen dioxide with iron(II)- and iron(III) cytochrome c
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Marked difference in cytochrome c oxidation mediated by HO· and/or O2·− free radicals in vitro
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Mechanism of peroxynitrite interaction with cytochrome c.
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“Recently Cassina et al. (2000) reported nitration of the heme-vicinal Tyr-67 of ferric cytochrome c treated by an excess of peroxynitrite.”
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“This means that protein nitration can affect enzyme activity, protein-protein interaction and phospho-tyrosine signalling pathways [6–12].”
BackgroundRecent Methodological Advances in the Analysis of Protein Tyrosine Nitration
Díaz‐Moreno, I., García-Heredia, J. M., González‐Arzola, K., Dı́az-Quintana, A., & la Rosa, M. Á. D. (2013) · ChemPhysChem · doi:10.1002/cphc.201300210 · Cited by 12
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“Nitration of cytochrome c by PN lead to conformational changes going hand in hand with altered redox properties including increased peroxidatic activity, resistance to reduction by ascorbate and different behavior in rat heart mitochondria [66].”
BackgroundCardiolipin interactions with cytochrome c increase tyrosine nitration yields and site-specificity
Demicheli, V., Tomasina, F., Sastre, S., Zeida, A., Tórtora, V., Lima, A. E., Batthyány, C., & Radí, R. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108824 · Cited by 12
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“Finally, peroxynitrite, the product of the reaction between superoxide and NO, inhibits mitochondrial respiration and induces cell apoptosis, which results in delayed neuronal death in the hippocampus([8,9]).”
BackgroundA Non‐damaging Method to Analyze the Configuration and Dynamics of Nitrotyrosines in Proteins
Díaz‐Moreno, I., Nieto, P. M., Conte, R. D., Gairí, M., García-Heredia, J. M., la Rosa, M. Á. D., & Dı́az-Quintana, A. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201103413 · Cited by 12
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“DAG and calcium serve to activate PKC, which can augment smooth muscle contraction directly through increasing intracellular calcium (45), decreasing activity of myosin light chain phosphatase (68), or increasing myofilament sensitization to calcium, independent of increases in cytosolic calcium concentration (32).”
BackgroundpH profile of cytochrome c-catalyzed tyrosine nitration.
Kambayashi, Y., Hitomi, Y., Kodama, N., Kubo, M., Okuda, J., Takemoto, K., Shibamori, M., Takigawa, T., & Ogino, K. (2006) · Acta Biochimica Polonica · doi:10.18388/abp.2006_3330 · Cited by 12
“Nitration, conformational change, and/or the decomposition of cytochrome c cause on increase in the peroxidase activity of cytochrome c (Cassina et al., 2000; Gębicka & Didik, 2003; 2005; Castro et al., 2004; Batthyány et al., 2005; Jang & Han, 2006).”
BackgroundNitrative Stress and Auditory Dysfunction
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“1997) and nitration (Balafanova et al. 2002; Cassina et al. 2000; Vadseth et al. 2004) may also be involved.”
BackgroundInfluentialReactivity of mitochondrial peroxiredoxins with biological hydroperoxides
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Metadata
- 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 › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology (medical) › 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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