Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins
Open accessAbstract
Oxygen and nitrogen centered reactive species can cause specific structural modifications in amino acids and proteins, such as the addition of a nitro group onto aromatic residues. Heretofore, studies on protein nitration have mainly focused on the in vitro and in vivo nitro addition to tyrosine residues (3-nitrotyrosine or 3NT), whereas the formation of nitrotryptophan in proteins in vivo and/or its functional significance has remained quite obscure. A novel structural modification, involving the addition of nitro and hydroxy groups to tryptophan, has been detected in the mitochondrial protein succinyl-CoA:3-oxoacid CoA transferase (SCOT) in rat heart. Modified SCOT accumulated progressively with age, which was associated with an elevation of its activity. The specific biochemical properties of this novel amino acid were characterized by a combination of HPLC-electrochemical detection and mass spectrometric analysis. This chapter describes the experimental steps involved in the characterizations and a procedure for the synthesis of nitrohydroxytryptophan. Similar methodology can be applied to the identification of nitrohydroxytryptophan in other proteins.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The effects of peroxynitrite on nitration of Tyr or Trp and S-nitrosylation of Cys likely depend on cellular status of antioxidants, various microenvironments including surface exposure, peptide loop structure, local charge groups, and the presence of competing amino acids nearby.
“The effects of peroxynitrite on nitration of Tyr or Trp and S-nitrosylation of Cys likely depend on cellular status of antioxidants, various microenvironments including surface exposure, peptide loop structure, local charge groups, and the presence of competing amino acids nearby (e.g., Cys near the potentially-nitrated Trp or Tyr), as suggested [98].”
Cites
Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease
Stadtman, E. R., & Berlett, B. S. (1998) · Drug Metabolism Reviews · doi:10.3109/03602539808996310 · Cited by 892 · see citing works
Beckman, J. S., Carson, M. A., Smith, C. D. L., & Koppenol, W. H. (1993) · Nature · doi:10.1038/364584a0 · Cited by 876 · see citing works
Greenacre, S., & Ischiropoulos, H. (2001) · Free Radical Research · doi:10.1080/10715760100300471 · Cited by 500 · see citing works
Sohal, R. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00856-0 · Cited by 477 · see citing works
Self-citationViner, R. I., Ferrington, D. A., Williams, T. D., Bigelow, D. J., & Schöneich, C. (1999) · Biochemical Journal · doi:10.1042/bj3400657 · Cited by 304 · see citing works
Widespread Nitration of Pathological Inclusions in Neurodegenerative Synucleinopathies
Duda, J. E., Giasson, B. I., Chen, Q., Gur, T., Hurtig, H. I., Stern, M. B., Gollomp, S. M., Ischiropoulos, H., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64781-5 · Cited by 276 · see citing works
Nitration of a peptide phytotoxin by bacterial nitric oxide synthase
Kers, J. A., Wach, M. J., Krasnoff, S. B., Widom, J., Cameron, K. D., Bukhalid, R. A., Gibson, D. M., Crane, B. R., & Loria, R. (2004) · Nature · doi:10.1038/nature02504 · Cited by 253 · see citing works
Kanski, J., Behring, A., Pelling, J., & Schöneich, C. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01030.2003 · Cited by 217 · see citing works
[19] Antibodies that recognize nitrotyrosine
Ye, Y. Z., Strong, M. J., Huang, Z., & Beckman, J. S. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69022-3 · Cited by 189 · see citing works
Kański, J., Hong, S. J., & Schöneich, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501773200 · Cited by 177 · see citing works
Sarver, A. L., Scheffler, N. K., Shetlar, M. D., & Gibson, B. W. (2001) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(01)00213-6 · Cited by 149 · see citing works
Proteomic identification of age-dependent protein nitration in rat skeletal muscle
Kański, J., Alterman, M. A., & Schöneich, C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00500-8 · Cited by 108 · see citing works
Myoglobin Scavenges Peroxynitrite without Being Significantly Nitrated
Herold, S., Kalinga, S., & Mehl, M. (2002) · Biochemistry · doi:10.1021/bi026046h · Cited by 65 · see citing works
Rebrin, I., Brégère, C., Kamzalov, S., Gallaher, T. K., & Sohal, R. S. (2007) · Biochemistry · doi:10.1021/bi7001482 · Cited by 49 · see citing works
Self-citationHong, S. J., Gokulrangan, G., & Schöneich, C. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.03.005 · Cited by 47 · see citing works
Ikeda, K., Hiraoka, B. Y., Iwai, H., Matsumoto, T., Mineki, R., Taka, H., Takamori, K., Ogawa, H., & Yamakura, F. (2006) · Nitric Oxide · doi:10.1016/j.niox.2006.04.263 · Cited by 43 · see citing works
Sharov, V. S., Galeva, N. A., Kański, J., Williams, T. D., & Schöneich, C. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.02.012 · Cited by 42 · see citing works
Critical overview of mitochondrial nitric-oxide synthase
Kato, K. (2006) · Frontiers in bioscience · doi:10.2741/2002 · Cited by 39 · see citing works
Ishii, Y., Ogara, A., Katsumata, T., Umemura, T., Nishikawa, A., Iwasaki, Y., Ito, R., Saito, K., Hirose, M., & Nakazawa, H. (2007) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2007.01.012 · Cited by 26 · see citing works
Thiagarajan, G., Lakshmanan, J., Chalasani, M., & Balasubramanian, D. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0929 · Cited by 22 · see citing works
Howard, J. B., Zieske, L. R., Clarkson, J., & Rathe, L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42430-6 · Cited by 21 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Human serum albumin: From bench to bedside
Fanali, G., di Masi, A., Trezza, V., Marino, M., Fasano, M., & Ascenzi, P. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.12.002 · Cited by 1,959 · see citing works
Reisz, J. A., Bansal, N., Qian, J. X., Zhao, W., & Furdui, C. M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5489 · Cited by 838 · see citing works
Abello, N., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Journal of Proteome Research · doi:10.1021/pr900039c · Cited by 359 · see citing works
Redox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises
Bachi, A., Dalle‐Donne, I., & Scaloni, A. (2012) · Chemical Reviews · doi:10.1021/cr300073p · Cited by 262 · see citing works
Amino acids: Chemistry, functionality and selected non-enzymatic post-translational modifications
Bischoff, R., & Schlüter, H. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.01.041 · Cited by 173 · see citing works
Ehrenshaft, M., Deterding, L. J., & Mason, R. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.003 · Cited by 158 · see citing works
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123 · see citing works
“, Cys near the potentially-nitrated Trp or Tyr), as suggested [98].”
BackgroundRedox modification of cell signaling in the cardiovascular system
Shao, D., Oka, S., Brady, C., Haendeler, J., Eaton, P., & Sadoshima, J. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.09.009 · Cited by 103 · see citing works
Perdivara, I., Deterding, L. J., Przybylski, M., & Tomer, K. B. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.02.016 · Cited by 100 · see citing works
Perrelli, A., Goitre, L., Salzano, A. M., Moglia, A., Scaloni, A., & Retta, S. F. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6015351 · Cited by 90 · see citing works
Functional Roles of Protein Nitration in Acute and Chronic Liver Diseases
Abdelmegeed, M. A., & Song, B. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/149627 · Cited by 62 · see citing works
Paviani, V., Queiroz, R. F., Marques, E. F., Mascio, P. D., & Augusto, O. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.015 · Cited by 50 · see citing works
Galetskiy, D., Lohscheider, J. N., Kononikhin, A. S., Popov, I. A., Николаев, Е. Н., & Adamska, I. (2010) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.4855 · Cited by 49 · see citing works
Bults, P., van de Merbel, N. C., & Bischoff, R. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1050384 · Cited by 44 · see citing works
Electrophilic characteristics and aqueous behavior of fatty acid nitroalkenes
Grippo, V., Mojović, M., Pavićević, A. A., Kabeláč, M., Hubatka, F., Tuřánek, J., Zatloukalová, M., Freeman, B. Α., & Vacek, J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101756 · Cited by 35 · see citing works
Characterization of lacrimal proline‐rich protein 4 ( PRR 4) in human tear proteome
Perumal, N., Funke, S., Pfeiffer, N., & Grus, F. H. (2014) · PROTEOMICS · doi:10.1002/pmic.201300039 · Cited by 34 · see citing works
Sain, H. M., Sharma, B., Jaggi, A. S., & Singh, N. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.07.002 · Cited by 32 · see citing works
Brégère, C., Rebrin, I., Gallaher, T. K., & Sohal, R. S. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.009 · Cited by 22 · see citing works
Self-citationCellular Redox, Epigenetics and Diseases
Goswami, S. K. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-4525-4_23 · Cited by 16 · see citing works
Effects of neutron radiation generated in deep space-like environments on food resources
Hatsuda, M., Kawasaki, H., Shigenaga, A., Taketani, A., Takanashi, T., Wakabayashi, Y., Otake, Y., Kamata, Y., Ichinose, A., Nishioka, H., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-38990-1 · Cited by 11 · see citing works
Reactive Nitrogen Species and Fibrinogen: Exploring the Effects of Nitration on Blood Clots
Nencini, F., Borghi, S., Giurranna, E., Barbaro, I., Taddei, N., Fiorillo, C., & Becatti, M. (2025) · Antioxidants · doi:10.3390/antiox14070825 · Cited by 8 · see citing works
Untargeted Discovery of Nitric Oxide-Modified Proteins
Deeb, R. S., Nuriel, T., & Gross, S. S. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-373866-0.00010-1 · Cited by 5 · see citing works
Wu, C.-Y., & Lu, C. (2014) · Journal of Chromatography A · doi:10.1016/j.chroma.2014.11.025 · Cited by 4 · see citing works
Alhalwani, A. Y., Davey, R. L., Repine, J. E., & Huffman, J. A. (2023) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2023.101447 · Cited by 4 · see citing works
Effect of phenolic-rich plant materials on protein and lipid oxidation reactions
Salminen, H. (2009) · Työväentutkimus Vuosikirja · Cited by 3 · see citing works
Mitochondrial Respiratory Function Decline in Aging and Life-Span Extension by Caloric Restriction
Wu, S., Wu, Y., Wang, C., Lee, W., & Wei, Y. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-602-3_7
- Authors
- Bregere, C., Rebrin, I., & Sohal, R. S.
- Affiliations
- University of Southern California (US)
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 2008
- Volume
- 441
- Pages
- 339-349
- ISSN
- 0076-6879 (ISSN-L)
- PMC
- PMC2821574
- OpenAlex
- W1583290442
- Cited by
- 28
- References
- 21
- Citations by year
- 2025: 1 · 2023: 2 · 2022: 1 · 2020: 1 · 2018: 1 · 2016: 1 · 2015: 3 · 2014: 5 · 2012: 3
- FWCI
- 4.31
- Type
- book chapter
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01 AG13563, R01AG013563)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- protein oxidation, nitrotyrosine, mitochondrial proteins, rat heart, aging, reactive oxygen species, reactive nitrogen species
- MeSH terms
- Animals, Humans, Nitrates, Oxidation-Reduction, Proteins, Tryptophan
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.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review