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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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Items 101–200 of 353
Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects
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“Native gel electrophoresis showed that peroxynitrite caused a dosedependent appearance of up to three different species, displaying decreased migration toward the cathode, indicating that each new species was more negatively charged, as expected for the various nitrated tyrosine-containing protein species (22).”
BackgroundInfluentialCampolo, N., Issoglio, F. M., Estrin, D. A., Bartesaghi, S., & Radí, R. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190052 · Cited by 84
Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration
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“MARCH5, a ubiquitin ligase in the outer membrane, associates with and ubiquitylates MFN1, MFN2, DRP1, and FIS1 (Yonashiro et al., 2006; Park et al., 2010).”
BackgroundInfluentialMitochondrial energy metabolism is markedly impaired by d-2-hydroxyglutaric acid in rat tissues
Latini, A., da Silva, C. G., Ferreira, G. C., Schuck, P. F., Scussiato, K., Sarkis, J. J., Dutra Filho, C. S., Wyse, A. T. S., Wannmacher, C. M. D., & Wajner, M. (2005) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2005.05.002 · Cited by 88
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“Our data are compatible with the findings that mutation [39], nitration [40, 41] or iodination [42] of Tyr67 drastically alters various heme-linked properties, suggesting that this residue plays an important role in heme ligation and catalytic activity.”
Self-citationGarcía-Heredia, J. M., Díaz‐Moreno, I., Nieto, P. M., Orzáez, M., Kocanis, S., Teixeira, M. S., Pérez‐Payá, E., Díaz-Quintana, A., & la Rosa, M. Á. D. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.009 · Cited by 81
“The effects of tyrosine nitration on protein function have been previously analysed using horse [4,14,16,18,19] and bovine [20] Cc.”
BackgroundInfluentialPeroxynitrite: cellular pathology and implications in autoimmunity
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Lipid Peroxyl Radicals Mediate Tyrosine Dimerization and Nitration in Membranes
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BackgroundSite-Selective Nitration of Tyrosine in Human Serum Albumin by Peroxynitrite
Jiao, K., Mandapati, S., Skipper, P. L., Tannenbaum, S. R., & Wishnok, J. S. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5118 · Cited by 76
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“The conversion of the low-spin state into the high-spin state occurred at concentrations higher than 1 mM, as judged by EPR spectral results (Figure 7). A similar profile was observed in cyt c by nitration [ 33 ], and was attributed to the loss of Met-80‐ haem-iron interactions [6].”
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Bailey, S. M., Landar, A. L., & Darley-Usmar, V. M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.011 · Cited by 73
The role of nitric oxide in prostaglandin biology; update
Kim, S. F. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.07.002 · Cited by 73
“aconitase, ATPase, and cytochrome c, further disrupting mitochondria respiratory function and consequently resulting in apoptosis [36; 39; 40].”
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“On the other hand, cytochrome c (43), fibrinogen (44), protein kinase Cε (45), and microsomal glutathione S-transferase 1 (46) present an increased functionality following PTM.”
BackgroundWong, P., Eiserich, J. P., Reddy, S., López, C. L., Cross, C. E., & van der Vliet, A. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2532 · Cited by 72
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Self-citationRemoval of H2O2 and generation of superoxide radical: Role of cytochrome c and NADH
Velayutham, M., Hemann, C. F., & Zweier, J. L. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.007 · Cited by 70
“The oxidation of the M80 heme ligand resulted in the increased peroxidase activity of Fecyt c [26,80].”
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Armani, C., Landini Jr., L., & Leone, A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787846973 · Cited by 68
Age-related decline in actomyosin structure and function
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Excitotoxins, Mitochondrial and Redox Disturbances in Multiple Sclerosis
Rajda, C., Pukoli, D., Bende, Z., Majláth, Z., & Vécsei, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020353 · Cited by 69
Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond
Demasi, M., Augusto, O., Bechara, E. J. H., Bicev, R. N., Cerqueira, F. M., da Cunha, F. M., Denicola, A., Gomes, F., Miyamoto, S., Netto, L. E. S., et al. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8176 · Cited by 71
Self-citation3-Nitrotyrosine Modified Proteins in Atherosclerosis
Thomson, L. (2015) · Disease Markers · doi:10.1155/2015/708282 · Cited by 65
“Protein nitration is a posttranslational modification caused by nitric oxide (NO) derived oxidants that frequently modifies the activity of the target molecule [15, 16].”
BackgroundSelf-citationMelatonin and Nitric Oxide: Two Required Antagonists for Mitochondrial Homeostasis
Acuña-Castroviejo, D., Escames, G., López, L. C., Hitos, A. B., & León, J. (2005) · Endocrine · doi:10.1385/endo:27:2:159 · Cited by 65
Mitochondrial Involvement in Amyotrophic Lateral Sclerosis: Trigger or Target?
Bacman, S. R., Bradley, W. G., & Moraes, C. T. (2006) · Molecular Neurobiology · doi:10.1385/mn:33:2:113 · Cited by 66
“It is known that chemical modifications, such as peroxinitration, reduce cytochrome-c function, inhibit respiration, and can stimulate apoptosis (99) and that cytochrome-c association with the IMM depends on the integrity of the membrane lipids—particularly on intact cardiolipin, an IMM lipid (100–102).”
BackgroundSrc kinases are important regulators of mitochondrial functions
Hébert-Chatelain, É. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.08.014 · Cited by 66
Armas, M. I. D., Esteves, R., Viera, N., Reyes, A. M., Mastrogiovanni, M., Alegria, T. G. P., Netto, L. E. S., Tórtora, V., Radí, R., & Trujillo, M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.451 · Cited by 65
The Role of Mitochondria in Brain Aging and the Effects of Melatonin
Escames, G., López, A., Garcia, J. A. D., Garcia, L., Acuña-Castroviejo, D., Garcia, J. J., & López, L. C. (2010) · Current Neuropharmacology · doi:10.2174/157015910792246245 · Cited by 62
“_ ) in mitochondria yielding peroxynitrite anion [126], which irreversible impairs the mitochondrial respiratory chain and decreases the efficiency of oxidative phosphorylation, leading to energy depletion and cell death [20, 25].”
BackgroundThe role of tobacco smoke induced mitochondrial damage in vascular dysfunction and atherosclerosis
Yang, Z., Harrison, C. M., Chuang, G. C., & Ballinger, S. W. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2007.02.010 · Cited by 64
Site-Specific Quantitation of Protein Nitration Using Liquid Chromatography/Tandem Mass Spectrometry
Willard, B. B., Ruse, C. I., Keightley, J. A., Bond, M., & Kinter, M. T. (2003) · Analytical Chemistry · doi:10.1021/ac034033j · Cited by 61
Diabetes triggers a PARP1 mediated death pathway in the heart through participation of FoxO1
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“Additionally, tyrosine nitration can directly activate cytochrome c, inactivate MnSOD, and initiate mitochondrial mediated cell death pathways [41,42].”
BackgroundVitturi, D. A., & Patel, R. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.037 · Cited by 59
“induced by Met-80 oxidation [77], Tyr-67 nitration [78], and interaction with anionic lipids such as cardiolipin [79].”
Cardiolipin activates cytochrome c peroxidase activity since it facilitates H2O2 access to heme
IuA, V., Proskurnina, E. V., Izmailov, D. Y., Novikov, A. A., Brusnichkin, A. V., Osipov, A. N., & Kagan, V. E. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906090082 · Cited by 59
Protein oxidation: role in signalling and detection by mass spectrometry
Spickett, C. M., & Pitt, A. R. (2012) · Amino Acids · doi:10.1007/s00726-010-0585-4 · Cited by 65
“…evidence that the formation of nitrotyrosine can alter protein activities, either as loss of function such as with Mn superoxide dismutase (Guo et al. 2003), or involving gain of function, which has been observed with protein kinase Ce and cytochrome c (Balafanova et al. 2002; Cassina et al. 2000).”
BackgroundProtective Effect of Metalloporphyrins against Cisplatin-Induced Kidney Injury in Mice
Pan, H., Shen, K., Wang, X., Meng, H., Wang, C., & Jin, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086057 · Cited by 58
“Peroxynitrite induces cytochrome c nitration at critical tyrosine-67 [46] and nitrated cytochrome c may be found in the cytosol of cells undergoing apoptosis [47].”
BackgroundProtein Nitration With Aging in the Rat Semimembranosus and Soleus Muscles
Fugere, N. A., Ferrington, D. A., & Thompson, L. V. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.8.806 · Cited by 57
“This scenario has been demonstrated in a few proteins, such as cytochrome c, which acquires a strong peroxidase activity after nitration (25).”
BackgroundDaiber, A., Daub, S., Bachschmid, M. M., Schildknecht, S., Oelze, M. W., Steven, S., Schmidt, P., Megner, A., Wada, M., Tanabe, T., et al. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14047542 · Cited by 58
“could also involve dityrosine formation [43,44], it has been demonstrated that reaction with peroxynitrite is catalyzed by the manganese cation [45].”
BackgroundNín, N., Cassina, A., Boggia, J. G., Alfonso, E., Botti, H., Peluffo, G., Trostchansky, A., Batthyány, C., Radí, R., Rubbo, H., et al. (2004) · Intensive Care Medicine · doi:10.1007/s00134-004-2427-x · Cited by 56
“Plasma or mitochondrial proteins were separated on a gel and electrophoretically transferred to nitrocellulose membranes as described before [ 31 ].”
MethodSelf-citationVenkatraman, A., Shiva, S., Davis, A. J., Bailey, S. M., Brookes, P. S., & Darley-Usmar, V. M. (2003) · Hepatology · doi:10.1053/jhep.2003.50293 · Cited by 55
Bhabak, K. P., & Mugesh, G. (2009) · Chemistry - A European Journal · doi:10.1002/chem.200902145 · Cited by 55
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Tempol protection of spinal cord mitochondria from peroxynitrite-induced oxidative damage
Xiong, Y., Singh, I. N., & Hall, E. D. (2009) · Free Radical Research · doi:10.1080/10715760902977432 · Cited by 55
“Nitration of cytochrome c results in a marked increase in its peroxidase activity, which may exacerbate the oxidative damage to mitochondrial proteins and membranes after PN exposure [43,51].”
McGreal, R., Kantorow, W. L., Chauss, D., Wei, J., Brennan, L., & Kantorow, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.04.004 · Cited by 54
Biochemical properties of cytochrome c nitrated by peroxynitrite
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Deficiency of Myeloperoxidase Increases Infarct Volume and Nitrotyrosine Formation in Mouse Brain
Takizawa, S., Aratani, Y., Fukuyama, N., Maeda, N., Hirabayashi, H., Koyama, H., Shinohara, Y., & Nakazawa, H. K. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200201000-00006 · Cited by 53
“…volume was increased in myeloperoxidase-deficient mice include the increased nitration of tyrosine residues of functionally crucial proteins, such as ribonucleotide reductase (Guittet et al., 2000), cytochrome c (Cassina et al., 2000), and c-SRC tyrosine kinase (MacMillan-Crow et al., 2000).”
BackgroundUnveiling the human nitroproteome: Protein tyrosine nitration in cell signaling and cancer
Griswold‐Prenner, I., Kashyap, A. K., Mazhar, S., Hall, Z. W., Fazelinia, H., & Ischiropoulos, H. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105038 · Cited by 52
“Nitration of mitochondrial protein participating in the tricarboxylic acid cycle, electron transport chain (ETC), primarily of cytochrome c (14), and antioxidant defenses (78–80) have been implicated in reduced mitochondrial functional capacity and disruption of metabolism.”
BackgroundSelf-citationZhang, Y., & Rosenberg, P. A. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02169.x · Cited by 52
“…nitrated by peroxynitrite, for example, ã 2002 Federation of European Neuroscience Societies, European Journal of Neuroscience, 16, 1015±1024 neuro®lament (Crow et al., 1997), MnSOD (MacMillan-Crow et al., 1996, 1998), tyrosine hydroxylase (Ara et al., 1998) and cytochrome c (Cassina et al., 2000).”
BackgroundChen, Y.-R., Chen, C.-L., Liu, X., Li, H., Zweier, J. L., & Mason, R. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.013 · Cited by 51
“As cyt c is present at a high concentration (~ 400 AM) in mitochondria [18,19], the results obtained from these in vitro studies implicate cyt c oxidation as an important biomarker of oxidative and inflammatory disease.”
ResultOn the Oxidation of Cytochrome c by Hypohalous Acids
Prütz, W. A., Kissner, R., Nauser, T., & Koppenol, W. H. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2321 · Cited by 51
Interplay Among Nitric Oxide and Reactive Oxygen Species
Zhao, J. H. (2007) · Plant Signaling & Behavior · doi:10.4161/psb.2.6.4802 · Cited by 50
Nitric oxide and cell signaling; modulation of redox tone and protein modification
Landar, A. L., & Darley-Usmar, V. M. (2003) · Amino Acids · doi:10.1007/s00726-003-0019-7 · Cited by 50
“drial respiratory function (Cassina et al., 2000).”
Tyrosine nitration as mediator of cell death
Franco, M. C., & Estévez, Á. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1662-8 · Cited by 50
Westbrook, D. G., Anderson, P. G., Pinkerton, K. E., & Ballinger, S. W. (2010) · Cardiovascular Toxicology · doi:10.1007/s12012-010-9085-8 · Cited by 49
“reactive oxygen- and nitrogen-mediated damage and alterations in function[11, 37–43].”
BackgroundRole of peroxidases in Parkinson disease: a hypothesis
Everse, J., & Coates, P. W. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.01.018 · Cited by 48
Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons
Pehar, M., Vargas, M. R., Robinson, K. M., Cassina, P., England, P., Beckman, J. S., Alzari, P. M., & Barbeito, L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.010 · Cited by 50
“Known examples include protein surfactant A [34], neurofilament-L [35], cytochrome c [36], fibrinogen [37], protein kinase Cε [38], and glutathione S-transferase [39].”
BackgroundPietraforte, D., Salzano, A. M., Marino, G., & Minetti, M. (2003) · Amino Acids · doi:10.1007/s00726-003-0021-0 · Cited by 48
“…that some cytochromes (Mehl et al., 1999; Zou et al., 2000; Daiber et al., 2000) are able to catalyze, rather than to protect, peroxynitrite-mediated tyrosine nitration of target molecules and=or to promote the nitration of its protein tyrosine residues (Cassina et al., 2000; Quijano et al., 2001).”
BackgroundInfluentialRole of nitric oxide in soybean cotyledon senescence
Jasid, S., Galatro, A., Villordo, J. J., Puntarulo, S., & Simontacchi, M. (2009) · Plant Science · doi:10.1016/j.plantsci.2009.02.007 · Cited by 47
Rodríguez-Roldán, V., García-Heredia, J. M., Navarro, J. A., la Rosa, M. Á. D., & Hervás, M. (2008) · Biochemistry · doi:10.1021/bi801329s · Cited by 47
Díaz‐Moreno, I., García-Heredia, J. M., Díaz-Quintana, A., Teixeira, M. S., & la Rosa, M. Á. D. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.09.012 · Cited by 46
“In addition, Tyr46 and Tyr48 are close to the heme group, which can catalyze the nitration reaction [10,33].”
BackgroundInfluentialSpecific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non‐functional apoptosome
García-Heredia, J. M., Díaz‐Moreno, I., Díaz-Quintana, A., Orzáez, M., Navarro, J. A., Hervás, M., & la Rosa, M. Á. D. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.12.007 · Cited by 45
“Nitrated Cc eluted at a much lower salt concentration than native protein because of the extra negative charge of deprotonated tyrosyl anions, whose pKa is modified by the strong electron-withdrawing effect of the substituent –NO2 group at the 3-position [24].”
BackgroundWheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochromecand Cardiolipin
Dı́az-Quintana, A., Pérez‐Mejías, G., Guerra‐Castellano, A., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6813405 · Cited by 47
“Several post-translational modifications modulate Cc structure and functionality, such as sulfoxidation [187], carbonylation [152], homocysteinylation [188], nitration [179, 180], and phosphorylation [189] (Figure 5).”
BackgroundRedox (phospho)lipidomics of signaling in inflammation and programmed cell death
Tyurina, Y. Y., Croix, C. M. S., Watkins, S. C., Watson, A. M., Epperly, M. W., Anthonymuthu, T. S., Kisin, E. R., Vlasova, I. I., Krysko, O., Krysko, D. V., et al. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir0119-004rr · Cited by 45
Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress
Jung, T., Engels, M., Klotz, L., Kröncke, K., & Grune, T. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.029 · Cited by 44
Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver
Zhu, J., Zhang, X., Roneker, C. A., McClung, J. P., Zhang, S., Thannhauser, T. W., Ripoll, D. R., Sun, Q., & Lei, X. G. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.018 · Cited by 41
Neurodegeneration and peroxidases
Everse, J., & Coates, P. W. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.10.007 · Cited by 42
Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease
Abate, G., Vezzoli, M., Sandri, M., Rungratanawanich, W., Memo, M., & Uberti, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111385 · Cited by 41
Post-Translational Modifications of Cytochrome c in Cell Life and Disease
Guerra‐Castellano, A., Márquez, I., Pérez‐Mejías, G., Dı́az-Quintana, A., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228483 · Cited by 41
“-NO2 and -NO primarily originate from RNS, such as peroxynitrite [119,125].”
BackgroundActivation of Microsomal Glutathione S-Transferase by Peroxynitrite
Ji, Y., & Bennett, B. M. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.1.136 · Cited by 41
Metabotropic glutamate receptor regulation of neuronal cell death
Berent‐Spillson, A. (2003) · Experimental Neurology · doi:10.1016/j.expneurol.2003.08.001 · Cited by 41
Carbone, D. L., Moreno, J. A., & Tjalkens, R. B. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.093 · Cited by 40
“Indeed, studies characterizing the effects of increased protein nitration have documented deleterious consequences including conformational changes (Cassina et al., 2000) and prevention of phosphorylation resulting in abnormal loss or gain of function, such as that reported for glutamine synthetase (Berlett et al.”
Perturbation of the Redox Site Structure of Cytochrome c Variants upon Tyrosine Nitration
Ly, H. K., Utesch, T., Díaz‐Moreno, I., García-Heredia, J. M., la Rosa, M. Á. D., & Hildebrandt, P. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp302301m · Cited by 41
Deletion of mouse MsrA results in HBO-induced cataract: MsrA repairs mitochondrial cytochrome c.
Brennan, L. A., Lee, W., Cowell, T. L., Giblin, F. J., & Kantorow, M. (2009) · Europe PMC (PubMed Central) · Cited by 40
Gu, X., Huang, Z., Ren, Z., Tang, X., Xue, R., Luo, X., Peng, S., Peng, H., Lü, B., Tian, J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01075 · Cited by 39
Hydroxyl radical oxidation of cytochrome c by aerobic radiolysis
Nukuna, B. N., Sun, G., & Anderson, V. E. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.004 · Cited by 39
Peroxynitrite efficiently mediates the interconversion of redox intermediates of myeloperoxidase
Furtmüller, P. G., Jantschko, W., Zederbauer, M., Schwanninger, M., Jakopitsch, C., Herold, S., Koppenol, W. H., & Obinger, C. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.138 · Cited by 39
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“Nitration of Tyr67 by ONOO- may result in secondary oxidation of Met80 [21].”
BackgroundAlonso, D. C., Encinas, J. M., UTTENTHAL, L. O., Boscá, L., Serrano, J., Fernández, A. P., Castro‐Blanco, S., Santacana, M., Bentura, M. L., Richart, A., et al. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00571-1 · Cited by 38
Nitration of PECAM-1 ITIM tyrosines abrogates phosphorylation and SHP-2 binding
Newman, D. K., Hoffman, S. M., Kotamraju, S., Zhao, T., Wakim, B. T., Kalyanaraman, B., & Newman, P. J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02060-0 · Cited by 37
“Nitration of a single tyrosine residue also affects the enzymatic activity of cytochrome c [30], whereas tyrosine nitration within tyrosine hydroxylase, the rate-limiting enzyme in dopamine synthesis, correlates with loss of enzymatic activity and a decline in dopamine levels [31].”
BackgroundOursler, M. J., Bradley, E. W., Elfering, S. L., & Giulivi, C. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00092.2004 · Cited by 37
“Similar conclusions were obtained by other groups: nitrated cytochrome c (obtained by tetranitromethane treatment) was six to seven times less efficient than the native one in restoring maximal respiration of cytochrome c-depleted mitochondria (52) or in sustaining state 4 respiration in intact heart mitochondria (8);…”
BackgroundRafikov, R., Rafikova, O., Aggarwal, S., Gross, C., Sun, X., Desai, J., Fulton, D., & Black, S. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.423269 · Cited by 36
“These include Complexes I and III of the electron transport chain (60–62), manganese-superoxide dismutase (MnSOD) (63, 64), cytochrome c (64, 65), mitochondrial creatine kinase (66, 67), and aconitase (68, 69).”
BackgroundBhabak, K. P., Vernekar, A. A., Jakka, S. R., Roy, G., & Mugesh, G. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob01234c · Cited by 36
Carbone, D. L., Popichak, K. A., Moreno, J. A., Safe, S. H., & Tjalkens, R. B. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.050781 · Cited by 36
“Indeed, studies characterizing the effects of increased protein nitration have documented deleterious consequences, including conformational changes (Cassina et al., 2000) and prevention of phosphorylation resulting in abnormal loss or gain of function, such as that reported for glutamine synthetase (Berlett et al.”
BackgroundZhang, C., Imam, S. Z., Ali, S. F., & Mayeux, P. R. (2002) · Nitric Oxide · doi:10.1016/s1089-8603(02)00003-4 · Cited by 35
Zhang, Y., Pu, H., Wang, Q., Cheng, S., Zhao, W., Zhang, Y., & Zhao, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706500200 · Cited by 35
Mitochondrial-nuclear Cross-talk in the Aging and Failing Heart
Marín-García, J., Pi, Y., & Goldenthal, M. J. (2006) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-006-0584-6 · Cited by 33
Nakagawa, H., Komai, N., Takusagawa, M., Miura, Y., Toda, T., Miyata, N., Ozawa, T., & Ikota, N. (2007) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.30.15 · Cited by 33
Yokozawa, T., Chen, C. P., Rhyu, D. Y., Tanaka, T., Park, J. C., & Kitani, K. (2002) · The Nephron journals/Nephron journals · doi:10.1159/000064483 · Cited by 33
Pietraforte, D., Salzano, A. M., Scorza, G., Marino, G., & Minetti, M. (2001) · Biochemistry · doi:10.1021/bi010998q · Cited by 32
Nitrocytochrome c: Synthesis, Purification, and Functional Studies
Souza, J. M., Castro, L., Cassina, A., Batthyány, C., & Radí, R. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01211-1 · Cited by 32
Self-citationPeroxynitrite and opiate antinociceptive tolerance: A painful reality
Salvemini, D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.11.005 · Cited by 31
“A1: Protein nitration and superoxide/peroxynitrite homeostasis—Several proteins are nitrated, a modification associated with loss, gain or change of function [90;91;92].”
BackgroundPhotoreceptor Mitochondrial Tyrosine Nitration in Experimental Uveitis
Wu, G., Lee, T. D., Moore, R. E., & Rao, N. A. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-1525 · Cited by 31
Reactive nitrogen species generated by heme proteins: Mechanism of formation and targets
Roncone, R., Barbieri, M., Monzani, E., & Casella, L. (2006) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2005.11.015 · Cited by 31
Zhang, F., Chen, L., Liu, C., Qiu, P., Wang, A., Li, L., & Wang, H. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.03.016 · Cited by 31
“Previous experiments indicated that nitration reactions can change protein function and conformation, inhibit tyrosine phosphorylation, and impose steric restrictions (Cassina et al., 2000; Balafanova et al., 2002).”
BackgroundTyrosine residues modification studied by MALDI-TOF mass spectrometry
Šantrůček, J., Strohalm, M., Kadlcik, V., Hynek, R., & Kodı́ček, M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.214 · Cited by 30
Nitration of tyrosine residues 368 and 345 in the β-subunit elicits FoF1-ATPase activity loss
Fujisawa, Y., Kato, K., & Giulivi, C. (2009) · Biochemical Journal · doi:10.1042/bj20090594 · Cited by 29
Boneh, A. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5585-2 · Cited by 29
Cytochrome c signalosome in mitochondria
Díaz‐Moreno, I., García-Heredia, J. M., Dı́az-Quintana, A., & la Rosa, M. Á. D. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0774-4 · Cited by 29
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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