Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences

Ehrenshaft, Marilyn; Deterding, Leesa J.; Mason, Ronald P.

doi:10.1016/j.freeradbiomed.2015.08.003

Cited by 158Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences

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Ehrenshaft, Marilyn, Deterding, Leesa J., Mason, Ronald P.·2015·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2015.08.003PMC PMC4684788

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Abstract

Proteins comprise a majority of the dry weight of a cell, rendering them a major target for oxidative modification. Oxidation of proteins can result in significant alterations in protein molecular mass such as breakage of the polypeptide backbone and/or polymerization of monomers into dimers, multimers, and sometimes insoluble aggregates. Protein oxidation can also result in structural changes to amino acid residue side chains, conversions that have only a modest effect on protein size but can have widespread consequences for protein function. There are a wide range of rate constants for amino acid reactivity, with cysteine, methionine, tyrosine, phenylalanine, and tryptophan having the highest rate constants with commonly encountered biological oxidants. Free tryptophan and tryptophan protein residues react at a diffusion-limited rate with hydroxyl radical and also have high rate constants for reactions with singlet oxygen and ozone. Although oxidation of proteins in general and tryptophan residues specifically can have effects detrimental to the health of cells and organisms, some modifications are neutral, whereas others contribute to the function of the protein in question or may act as a signal that damaged proteins need to be replaced. This review provides a brief overview of the chemical mechanisms by which tryptophan residues become oxidized, presents both the strengths and the weaknesses of some of the techniques used to detect these oxidative interactions, and discusses selected examples of the biological consequences of tryptophan oxidation in proteins from animals, plants, and microbes.

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Trp• reacts very rapidly with O2•− with second-order rate constants k in the range 0.7-2.2 × 10^9 M−1 s−1, mainly giving hydroperoxides in almost quantitative yields.
“Trp• reacts very rapidly with O2•− with second order rate constants, k, in the range 0.7–2.2 × 109 M−1 s−1, the main initial products being hydroperoxides, in almost quantitative yields [145,146,147,148,149,150,151], Figure 56.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [145]

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Beyond Cholesterol
Epstein, F. H., Steinberg, D. I., Parthasarathy, S., Carew, T. E., Khoo, J. C., & Witztum, J. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198904063201407 · Cited by 6,425 · see citing works
Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
Stadtman, E. R., & Levine, R. L. (2003) · Amino Acids · doi:10.1007/s00726-003-0011-2 · Cited by 1,968 · see citing works
Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids.
Steinbrecher, U. P., Parthasarathy, S., Leake, D. S., Witztum, J. L., & Steinberg, D. I. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3883 · Cited by 1,626 · see citing works
Ion Suppression in Mass Spectrometry
Annesley, T. M. (2003) · Clinical Chemistry · doi:10.1373/49.7.1041 · Cited by 1,598 · see citing works
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392 · see citing works
Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269 · see citing works
Proteomics by Mass Spectrometry: Approaches, Advances, and Applications
Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078 · see citing works
Singlet oxygen-mediated damage to proteins and its consequences
Davies, M. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00817-9 · Cited by 996 · see citing works
Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
Mann, M., Ong, S. E., Grønborg, M., Steen, H., Jensen, O. N., & Pandey, A. (2002) · Trends in biotechnology · doi:10.1016/s0167-7799(02)01944-3 · Cited by 901 · see citing works
Shotgun identification of protein modifications from protein complexes and lens tissue
MacCoss, M. J., McDonald, W. H., Saraf, A., Sadygov, R. G., Clark, J., Tasto, J. J., Gould, K. L., Wolters, D. A., Washburn, M. P., Weiss, A., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122231399 · Cited by 593 · see citing works
Alpha-crystallin
Horwitz, J. (2003) · Experimental Eye Research · doi:10.1016/s0014-4835(02)00278-6 · Cited by 587 · see citing works
Photo-oxidation of proteins
Pattison, D. I., Rahmanto, A. S., & Davies, M. J. (2011) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05164d · Cited by 577 · see citing works
Peroxynitrite reactivity with amino acids and proteins
Alvarez, B., & Radi, R. (2003) · Amino Acids · doi:10.1007/s00726-003-0018-8 · Cited by 560 · see citing works
Reactive species formed on proteins exposed to singlet oxygen
Davies, M. J. (2004) · Photochemical & Photobiological Sciences · doi:10.1039/b307576c · Cited by 399 · see citing works
Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene
Andersen, P. M. (2006) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-996-0008-9 · Cited by 368 · see citing works
Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages
Hazell, L. J., & Stocker, R. (1993) · Biochemical Journal · doi:10.1042/bj2900165 · Cited by 311 · see citing works
Preparation of Proteins and Peptides for Mass Spectrometry Analysis in a Bottom‐Up Proteomics Workflow
Gundry, R. L., White, M. Y., Murray, C. I., Kane, L. A., Fu, Q., Stanley, B. A., & Eyk, J. E. V. (2009) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb1025s88 · Cited by 307 · see citing works
Mechanisms of oxidative damage of low density lipoprotein in human atherosclerosis
Heinecke, J. W. (1997) · Current Opinion in Lipidology · doi:10.1097/00041433-199710000-00005 · Cited by 275 · see citing works
Reaction of ozone with amino acids and proteins
Mudd, J. B., Leavitt, R. I., Ongun, A., & McManus, T. T. (1969) · Atmospheric Environment (1967) · doi:10.1016/0004-6981(69)90024-9 · Cited by 255 · see citing works
Singlet-oxygen-mediated amino acid and protein oxidation: Formation of tryptophan peroxides and decomposition products
Gracanin, M., Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.015 · Cited by 252 · see citing works
Consequences of Total and Subtotal Myeloperoxidase Deficiency: Risk or Benefit ?
Kutter, D., Devaquet, P., Vanderstocken, G., Paulus, J., Marchal, V., & Gothot, A. (2000) · Acta Haematologica · doi:10.1159/000041062 · Cited by 250 · see citing works
The global burden of cataract
Rao, G. N., Khanna, R., & Payal, A. R. (2010) · Current Opinion in Ophthalmology · doi:10.1097/icu.0b013e3283414fc8 · Cited by 215 · see citing works
Techniques for phosphopeptide enrichment prior to analysis by mass spectrometry
Dunn, J. D., Reid, G. E., & Bruening, M. L. (2009) · Mass Spectrometry Reviews · doi:10.1002/mas.20219 · Cited by 213 · see citing works
Myeloperoxidase, modified lipoproteins, and atherogenesis
Nicholls, S. J., & Hazen, S. L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800086-jlr200 · Cited by 209 · see citing works
Kinetics of ozonation. 2. Amino acids and model compounds in water and comparisons to rates in nonpolar solvents
Pryor, W. A., Giamalva, D. H., & Church, D. F. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00335a038 · Cited by 204 · see citing works
Identification of tryptophan oxidation products in bovine α‐crystallin
Finley, E. L., Dillon, J. P., Crouch, R. K., & Schey, K. L. (1998) · Protein Science · doi:10.1002/pro.5560071116 · Cited by 194 · 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
Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS
Gros‐Louis, F., Soucy, G., Larivière, R., & Julien, J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06683.x · Cited by 189 · see citing works
Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping
Mason, R. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.077 · Cited by 170 · see citing works
Self-citation
Post-Translational Modifications in the Nuclear Region of Young, Aged, and Cataract Human Lenses
Hains, P. G., & Truscott, R. J. W. (2007) · Journal of Proteome Research · doi:10.1021/pr070138h · Cited by 170 · see citing works
Guidelines for tunneling in enzymes
Moser, C. C., Anderson, J. L. R., & Dutton, P. L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.441 · Cited by 162 · see citing works
Changes in Structures of Milk Proteins upon Photo-oxidation
Dalsgaard, T. K., Otzen, D. E., Nielsen, J. H., & Larsen, L. B. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf071948g · Cited by 154 · see citing works
The Molecular Mechanism for the Genetic Disorder Familial Defective Apolipoprotein B100
Borén, J., Ekström, U., Agren, B., Nilsson‐Ehle, P., & Innerarity, T. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008890200 · Cited by 147 · see citing works
Peroxidic intermediates in photosensitized oxygenation of tryptophan derivatives
Saito, I., Matsuura, T., Nakagawa, M., & Hino, T. (1977) · Accounts of Chemical Research · doi:10.1021/ar50117a006 · Cited by 142 · see citing works
Tryptophan Oxidation by Singlet Molecular Oxygen [O2(1Δg)]: Mechanistic Studies Using18O-Labeled Hydroperoxides, Mass Spectrometry, and Light Emission Measurements
Ronsein, G. E., Oliveira, M. C. B., Miyamoto, S., Medeiros, M. H. G., & Di Mascio, P. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800026g · Cited by 142 · see citing works
Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates.
Kelman, D. J., DeGray, J. A., & Mason, R. P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37308-8 · Cited by 139 · see citing works
Self-citation
Electron transfer in peptides and proteins
Giese, B., Graber, M. C., & Cordes, M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.08.026 · Cited by 123 · see citing works
Reaction of Singlet Oxygen with Tryptophan in Proteins: A Pronounced Effect of the Local Environment on the Reaction Rate
Jensen, R. L., Arnbjerg, J., & Ogilby, P. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303710m · Cited by 121 · see citing works
Fluorescence Characteristics of Kynurenine and N′-Formylkynurenine, Their Use as Reporters of the Environment of Tryptophan 62 in Hen Egg-White Lysozyme1
Fukunaga, Y., Katsuragi, Y., Izumi, T., & Sakiyama, F. (1982) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a133909 · Cited by 121 · see citing works
The hydroxylation of tryptophan
Maskos, Z., Rush, J. D., & Koppenol, W. H. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90605-v · Cited by 111 · see citing works
Bicarbonate-dependent Peroxidase Activity of Human Cu,Zn-Superoxide Dismutase Induces Covalent Aggregation of Protein
Zhang, H., Andrekopoulos, C., Joseph, J., Chandran, K., Karoui, H., Crow, J. P., & Kalyanaraman, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302051200 · Cited by 108 · see citing works
Self-peroxidation of Metmyoglobin Results in Formation of an Oxygen-reactive Tryptophan-centered Radical
Gunther, M. R., Kelman, D. J., Corbett, J. T., & Mason, R. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16075 · Cited by 108 · see citing works
Self-citation
Peroxidation of a Specific Tryptophan of Metmyoglobin by Hydrogen Peroxide
DeGray, J. A., Gunther, M. R., Tschirret-Guth, R. A., de Montellano, P. R. O., & Mason, R. P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2359 · Cited by 107 · see citing works
Self-citation
Identification of oxidation products and free radicals of tryptophan by mass spectrometry
Domingues, M. R., Domingues, P. M., Reis, A., Fonseca, C., Amado, F. M. L., & Ferrer-Correia, A. J. V. (2003) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(03)00127-2 · Cited by 101 · see citing works
Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
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
Self-citation
Formation of Lysine-Derived Oxidation Products and Loss of Tryptophan during Processing of Porcine Patties with Added Avocado Byproducts
Utrera, M., Rodríguez-Carpena, J. G., Morcuende, D., & Estévez, M. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf3001313 · Cited by 99 · see citing works
Detection and reactions of the globin radical in haemoglobin
McArthur, K. M., & Davies, M. J. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90002-9 · Cited by 91 · see citing works
Tryptophan 32 Potentiates Aggregation and Cytotoxicity of a Copper/Zinc Superoxide Dismutase Mutant Associated with Familial Amyotrophic Lateral Sclerosis
Taylor, D. M., Gibbs, B. F., Kabashi, E., Minotti, S., Durham, H. D., & Agar, J. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610119200 · Cited by 85 · see citing works
Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation
Sancataldo, G., Vetri, V., Foderà, V., Cara, G. D., Militello, V., & Leone, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084552 · Cited by 79 · see citing works
Localization of non-essential tryptophan residues for the biological activity of lysozymet
Previero, A., Coletti‐Previero, M., & Jollès, P. (1967) · Journal of Molecular Biology · doi:10.1016/0022-2836(67)90331-2 · Cited by 77 · see citing works
Protein nitrotryptophan: Formation, significance and identification
Nuriel, T., Hansler, A., & Gross, S. S. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.032 · Cited by 77 · see citing works
Characterization of O2 (1Δg)-derived oxidation products of tryptophan: A combination of tandem mass spectrometry analyses and isotopic labeling studies
Ronsein, G. E., de Oliveira, M. C. B., de Medeiros, M. H. G., & Mascio, P. D. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.08.016 · Cited by 76 · see citing works
N-Formylkynurenine as a Marker of High Light Stress in Photosynthesis
Dreaden, T. M., Chen, J., Rexroth, S., & Barry, B. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.212928 · Cited by 75 · see citing works
Atmospheric pressure ionization time-of-flight mass spectrometry coupled with fast liquid chromatography for quantitation and accurate mass measurement of five pharmaceutical drugs in human plasma
Zhang, H., Heinig, K., & Henion, J. D. (2000) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(200003)35:3 · Cited by 69 · see citing works
A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity
Medinas, D. B., Gozzo, F. C., Santos, L. F. A., Iglesias, A. H., & Augusto, O. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.018 · Cited by 67 · see citing works
A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide
Gunther, M. R., Sturgeon, B. E., & Mason, R. P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00164-7 · Cited by 66 · see citing works
Self-citation
Formation of N‐formylkynurenine suggests the involvement of apolipoprotein B‐100 centered tryptophan radicals in the initiation of LDL lipid peroxidation
Gieβauf, A., van Wickern, B., Simat, T. J., Steinhart, H., & Esterbauer, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00546-7 · Cited by 66 · see citing works
Unraveling the different proteomic platforms
Messana, I., Cabras, T., Iavarone, F., Vincenzoni, F., Urbani, A., & Castagnola, M. (2012) · Journal of Separation Science · doi:10.1002/jssc.201200830 · Cited by 64 · see citing works
Photooxidation of Lens α-Crystallin by Hypericin (Active Ingredient in St. John's Wort)¶
Schey, K. L., Ouvry‐Patat, S. A., Chignell, C. F., Datillo, M., Wang, R. H., & Roberts, J. E. (2000) · Photochemistry and Photobiology · doi:10.1562/0031-8655(2000)0720200polcbh2.0.co2 · Cited by 61 · see citing works
Immunological detection of N-formylkynurenine in oxidized proteins
Ehrenshaft, M., Silva, S. D. O., Perdivara, I., Bilski, P. J., Sik, R. H., Chignell, C. F., Tomer, K. B., & Mason, R. P. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.020 · Cited by 60 · see citing works
Self-citation
Myeloperoxidase-derived oxidants modify apolipoprotein A-I and generate dysfunctional high-density lipoproteins: comparison of hypothiocyanous acid (HOSCN) with hypochlorous acid (HOCl)
Hadfield, K. A., Pattison, D. I., Brown, B. E., Hou, L., Rye, K., Davies, M. J., & Hawkins, C. L. (2012) · Biochemical Journal · doi:10.1042/bj20121210 · Cited by 59 · see citing works
Immuno-spin trapping from biochemistry to medicine: Advances, challenges, and pitfalls. Focus on protein-centered radicals
Gomez-Mejiba, S., Zhai, Z., Vedova, M. C. D., Munoz, M. D., Chatterjee, S., Towner, R. A., Hensley, K., Floyd, R. A., Mason, R. P., & Ramírez, D. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.039 · Cited by 52 · see citing works
Self-citation
Human Low Density Lipoprotein as a Target of Hypochlorite Generated by Myeloperoxidase
Jerlich, A., Fabjan, J. S., Tschabuschnig, S., Smirnova, A. V., Horáková, Ľ., Hayn, M., Auer, H., Guttenberger, H., Leis, H., Tatzber, F., et al. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00439-5 · Cited by 52 · see citing works
An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE
Helland, R., Fjellbirkeland, A., Karlsen, O. A., Ve, T., Lillehaug, J. R., & Jensen, H. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800340200 · Cited by 51 · see citing works
Photooxidation of specific residues in .alpha.-crystallin polypeptides
McDermott, M. J., Chiesa, R., Roberts, J. E., & Dillon, J. P. (1991) · Biochemistry · doi:10.1021/bi00099a023 · Cited by 46 · see citing works
l -Tryptophan Radical Cation Electron Spin Resonance Studies: Connecting Solution-Derived Hyperfine Coupling Constants with Protein Spectral Interpretations
Connor, H. D., Sturgeon, B. E., Mottley, C., Sipe, H. J., & Mason, R. P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja0780277 · Cited by 46 · see citing works
Self-citation
Computational Study on the Attack of .OH Radicals on Aromatic Amino Acids
Mujika, J. I., Uranga, J., & Matxain, J. M. (2013) · Chemistry – A European Journal · doi:10.1002/chem.201203862 · Cited by 45 · see citing works
Protein oxidation: identification and utilisation of molecular markers to differentiate singlet oxygen and hydroxyl radical-mediated oxidative pathways
Plowman, J. E., Deb‐Choudhury, S., Grosvenor, A. J., & Dyer, J. M. (2013) · Photochemical & Photobiological Sciences · doi:10.1039/c3pp50182e · Cited by 44 · see citing works
Atmospheric pressure ion mobility spectrometry of protonated and sodiated peptides
Wu, C., Klasmeier, J., & Hill, H. H. (1999) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(19990630)13:12 · Cited by 43 · see citing works
Identification of Modified Tryptophan Residues in Apolipoprotein B-100 Derived from Copper Ion-Oxidized Low-Density Lipoprotein
Yang, C., Gu, Z., Yang, M., Lin, S., Siuzdak, G. E., & Smith, C. V. (1999) · Biochemistry · doi:10.1021/bi991464g · Cited by 41 · see citing works
Specific Racemization and Isomerization of the Aspartyl Residue of αA-Crystallin Due to UV-B Irradiation
Fujii, N., Momose, Y., Ishibashi, Y., Uemura, T., Takita, M., & Takehana, M. (1997) · Experimental Eye Research · doi:10.1006/exer.1997.0315 · Cited by 40 · see citing works
Light-Induced Oxidative Stress, N-Formylkynurenine, and Oxygenic Photosynthesis
Kasson, T. M. D., Rexroth, S., & Barry, B. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042220 · Cited by 40 · see citing works
Comparison of low-density lipoprotein modification by myeloperoxidase-derived hypochlorous andhypobromous acids
Carr, A. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00552-4 · Cited by 38 · see citing works
Mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase
Zhang, H., Joseph, J., Crow, J. P., & Kalyanaraman, B. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.026 · Cited by 38 · see citing works
In Vivo Inactivation of Lysozyme by Ozone
Holzman, R. S., Gardner, D. E., & Coffin, D. L. (1968) · Journal of Bacteriology · doi:10.1128/jb.96.5.1562-1566.1968 · Cited by 36 · see citing works
Oxidative stress induces protein and DNA radical formation in follicular dendritic cells of the germinal center and modulates its cell death patterns in late sepsis
Chatterjee, S., Lardinois, O. M., Bhattacharjee, S., Tucker, J., Corbett, J. T., Deterding, L. J., Ehrenshaft, M., Bonini, M. G., & Mason, R. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.037 · Cited by 34 · see citing works
Self-citation
Reactive oxygen and oxidative stress: N-formyl kynurenine in photosystem II and non-photosynthetic proteins
Dreaden, T. M., & Barry, B. A. (2012) · Photosynthesis Research · doi:10.1007/s11120-012-9784-z · Cited by 34 · see citing works
Using Tandem Mass Spectrometry to Quantify Site‐Specific Chlorination and Nitration of Proteins: Model System Studies with High‐Density Lipoprotein Oxidized by Myeloperoxidase
Shao, B., & Heinecke, J. W. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)00803-8 · Cited by 32 · see citing works
Direct Evidence for apo B-100-Mediated Copper Reduction: Studies with Purified apo B-100 and Detection of Tryptophanyl Radicals
Batthyány, C., Santos, C. X. C., Botti, H., Červeñanský, C., Radí, R., Augusto, O., & Rubbo, H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2102 · Cited by 32 · see citing works
Detection and Characterization of Peroxynitrite-Induced Modifications of Tyrosine, Tryptophan, and Methionine Residues by Tandem Mass Spectrometry
Rebrin, I., Brégère, C., Gallaher, T. K., & Sohal, R. S. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01215-9 · Cited by 30 · see citing works
Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins
Bregere, C., Rebrin, I., & Sohal, R. S. (2008) · Methods in Enzymology · doi:10.1016/s0076-6879(08)01219-6 · Cited by 28 · see citing works
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Cold atmospheric Plasma Jet-Generated Oxidized Derivatives of Tryptophan and Their Selective Effects on Murine Melanoma and Fibroblast Cells
Li, X., Feng, Z., Pu, S., Yang, Y., Shi, X., & Zhao, X. (2018) · Plasma Chemistry and Plasma Processing · doi:10.1007/s11090-018-9910-6 · Cited by 15 · see citing works
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Figueroa, J. D., Barroso-Torres, N., Morales, M., Herrera, B., Aranda, M., Dorta, E., & López‐Alarcón, C. (2023) · Foods · doi:10.3390/foods12234360 · Cited by 14 · see citing works
Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer
Kovaĺ, T., Švecová, L., Østergaard, L., Skálová, T., Dušková, J., Hašek, J., Kolenko, P., Fejfarová, K., Stránský, J., Trundová, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50105-3 · Cited by 14 · see citing works
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Marchelak, A., Kołodziejczyk-Czepas, J., Wasielewska, P., Nowak, P., & Olszewska, M. A. (2021) · Antioxidants · doi:10.3390/antiox10040581 · Cited by 14 · see citing works
Porphyrin-polyethylenimine conjugates as photodynamic polymers to eliminate Staphylococcus aureus and Escherichia coli
Boarini, M. B., Gsponer, N. S., Milanesio, M. E., & Durantini, E. N. (2023) · European Polymer Journal · doi:10.1016/j.eurpolymj.2023.112512 · Cited by 13 · see citing works
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Palacios, Y. B., Simonetti, S. O., Chavez, C. H., Álvarez, M. G., Cordero, P. V., Cuello, E. A., López, E. J. G., Larghi, E. L., Agazzi, M. L., Durantini, E. N., et al. (2025) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2025.113105 · Cited by 13 · see citing works
Fullerene C60-chitosan conjugate applied in the photoinactivation of Staphylococcus aureus
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Graham, R. J., Ketcham, S. A., Mohammad, A., Paregol, E., Yoon, S., Zou, G., Ju, T., Faustino, P. J., Ashraf, M., & Madhavarao, C. N. (2021) · Biochemical Engineering Journal · doi:10.1016/j.bej.2021.107928 · Cited by 11 · see citing works
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Baigorria, E., Durantini, J. E., Palma, M. A. D., Gsponer, N. S., Milanesio, M. E., & Durantini, E. N. (2021) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-021-00074-2 · Cited by 12 · see citing works
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Escobar‐Álvarez, E., Leinisch, F., Araya, G., Monasterio, O., Lorentzen, L. G., Silva, E., Davies, M. J., & López‐Alarcón, C. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.014 · Cited by 12 · see citing works
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Bikaki, M., & Kuhnert, N. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b01056 · Cited by 12 · see citing works
Oxidative Post-translational Protein Modifications upon Ischemia/Reperfusion Injury
Binek, A., Castans, C., Jorge, I., Bagwan, N., Rodrı́guez, J. M., Fernández‐Jiménez, R., Galán‐Arriola, C., Oliver, E., Gómez, M., Clemente‐Moragón, A., et al. (2024) · Antioxidants · doi:10.3390/antiox13010106 · Cited by 10 · see citing works
Structure and Function of Tryptophan–Tyrosine Dyads in Biomimetic β Hairpins
McCaslin, T. G., Pagba, C. V., Chi, S., Hwang, H. J., Gumbart, J. C., Perry, J. W., Olivieri, C., Porcelli, F., Veglia, G., Guo, Z., et al. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b12452 · Cited by 11 · see citing works
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Đukić, T., Smiljanić, K., Mihailović, J. M., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Veličković, T. Ć. (2022) · Foods · doi:10.3390/foods11243993 · Cited by 11 · see citing works
Chemical engineering of protein cages and nanoparticles for pharmaceutical applications
Aljabali, A. A. A., Zoubi, M. S. A., Alzoubi, L., Al‐Batayneh, K., Obeid, M. A., & Tambuwala, M. M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-820702-4.00017-9 · Cited by 11 · see citing works
Multifarious analytical capabilities of the UV/Vis protein fluorescence in blood plasma
Gayer, A. V., Yakimov, B. P., Sluchanko, N. N., & Shirshin, E. A. (2022) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2022.122028 · Cited by 10 · see citing works
Analysis of the Propionate Metabolism in Bacillus subtilis during 3-Indolacetic Production
Castillo-Alfonso, F., Quintana-Menéndez, A., Vigueras-Ramírez, G., Sales‐Cruz, M., Rosales-Colunga, L. M., & Olivares‐Hernández, R. (2022) · Microorganisms · doi:10.3390/microorganisms10122352 · Cited by 8 · see citing works
Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants
Zhou, L., Zhang, M., Cheng, J., Wang, Z., Guo, Z., & Li, B. (2022) · CyTA - Journal of Food · doi:10.1080/19476337.2022.2107705 · Cited by 8 · see citing works
The Different Colors of mAbs in Solution
Ambrogelly, A. (2021) · Antibodies · doi:10.3390/antib10020021 · Cited by 8 · see citing works
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Pérez, M. E., Durantini, J. E., Martínez, S. R., Durantini, A. M., Milanesio, M. E., & Durantini, E. N. (2024) · ChemBioChem · doi:10.1002/cbic.202400138 · Cited by 7 · see citing works
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Gowthami, N., Pursotham, N., Dey, G., Ghose, V., Sathe, G. J., Pruthi, N., Shukla, D. P., Gayathri, N., Santhoshkumar, R., Padmanabhan, B., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15953 · Cited by 7 · see citing works
Effect of Boiling Treatment on Linoleic Acid-Induced Oxidation of Myofibrillar Protein in Grass Carp
Liu, M., Li, F., Tang, Y., Zhao, J., Lei, X., & Ming, J. (2024) · Foods · doi:10.3390/foods13244153 · Cited by 6 · see citing works
Micellar Solvent Accessibility of Esterified Polyoxyethylene Chains as Crucial Element of Polysorbate Oxidation: A Density Functional Theory, Molecular Dynamics Simulation and Liquid Chromatography/Mass Spectrometry Investigation
Weber, J., Pedri, L., Peters, L. P., Quoika, P. K., Dinu, D. F., Liedl, K. R., Tautermann, C. S., Diederichs, T., & Garidel, P. (2025) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.4c01015 · Cited by 6 · see citing works
BODIPY-Loaded ZIF-8 Nanomaterials for Enhanced Photodynamic Inactivation of Staphylococcus aureus
Pérez, M. E., Durantini, J. E., Milanesio, M. E., & Durantini, E. N. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c00787 · Cited by 6 · see citing works
Development of a high throughput oxidation profiling strategy for monoclonal antibody products
Fischer, P. L., Merkel, O. M., Siedler, M., & Huelsmeyer, M. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114301 · Cited by 6 · see citing works
Integrating time since deposition estimation of bloodstains into a DNA profiling workflow: A novel approach using fluorescence spectroscopy
Elliott, C. I., Simmons, D. B. D., & Stotesbury, T. E. (2024) · Talanta · doi:10.1016/j.talanta.2024.127234 · Cited by 6 · see citing works

Probing the Tryptophan Environment in Therapeutic Proteins: Implications for Higher Order Structure on Tryptophan Oxidation
Barnett, G. V., Balakrishnan, G., Chennamsetty, N., Hoffman, L., Bongers, J., Tao, L., Huang, Y., Slaney, T., Das, T. K., Leone, A., et al. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.12.027 · Cited by 33 · see citing works
Singlet-oxygen-mediated amino acid and protein oxidation: Formation of tryptophan peroxides and decomposition products
Gracanin, M., Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.015 · Cited by 252 · see citing works
Ditryptophan Cross-Links as Novel Products of Protein Oxidation
Paviani, V., Galdino, G. T., dos Prazeres, J. N., Queiroz, R. F., & Augusto, O. (2017) · Journal of the Brazilian Chemical Society · doi:10.21577/0103-5053.20170239 · Cited by 22 · see citing works
Quantitative evaluation of tryptophan oxidation in actin and troponin I from skeletal muscles using a rat model of acute oxidative stress
Fedorova, M., Todorovski, T., Кулева, Н. В., & Hoffmann, R. (2010) · PROTEOMICS · doi:10.1002/pmic.201000147 · Cited by 36 · see citing works
Superoxide radicals react with peptide-derived tryptophan radicals with very high rate constants to give hydroperoxides as major products
Carroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.033 · Cited by 48 · see citing works

Authors: Ehrenshaft, M., Deterding, L. J., & Mason, R. P.
Affiliations: National Institutes of Health (US)
Corresponding author: Ehrenshaft, Marilyn
ORCID: Deterding, Leesa J.
Mason, Ronald P.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2015-12
Volume: 89
Pages: 220-228
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2015.08.003
PMC: PMC4684788
OpenAlex: W2187856084
Cited by: 158
References: 95
Citations by year: 2026: 16 · 2025: 13 · 2024: 15 · 2023: 20 · 2022: 16 · 2021: 22 · 2020: 15 · 2019: 15 · 2018: 14 · 2017: 6 · 2016: 6
FWCI: 0.84
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Environmental Health Sciences
National Institutes of Health
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 › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: tryptophan oxidation, protein oxidative modification, reactive oxygen species, hydroxyl radicals, singlet oxygen, ozone, protein aggregation, protein misfolding, protein function
MeSH terms: Animals, Humans, Oxidation-Reduction, Proteins, Mass Spectrometry, Tryptophan, Reactive Oxygen Species

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Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences

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