Free radical-mediated oxidation of free amino acids and amino acid residues in proteins

Amino Acids

Volumn 25, Issue 3-4, 2003, Pages 207-218

  Stadtman, E R ^a   Levine, R L ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

Methionine oxidation reduction; Oxidized protein proteolysis; Oxygen free radicals; Protein carbonyls

Indexed keywords

ALIPHATIC COMPOUND; AMINO ACID; AMINO ACID DERIVATIVE; AROMATIC AMIDE; CARBOHYDRATE DERIVATIVE; CARBONYL DERIVATIVE; CYSTEINE; FREE RADICAL; METHIONINE; METHIONINE DERIVATIVE; POLYPEPTIDE; POLYUNSATURATED FATTY ACID; PROTEIN; REACTIVE OXYGEN METABOLITE; SULFUR AMINO ACID; THIOL DERIVATIVE;

AMINO ACID ANALYSIS; ANTIOXIDANT ACTIVITY; CHLORINATION; ENZYME REGULATION; GLYCATION; HEREDITY; HYDROXYLATION; LIFESTYLE; NITRATION; NITROSYLATION; OXIDATION; OXIDATION KINETICS; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; REACTION ANALYSIS; REVIEW; SULFOXIDATION;

AMINO ACIDS; FREE RADICALS; HUMANS; METALS; OXIDATION-REDUCTION; PROTEINS; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN SPECIES;

EID: 0346100345     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-003-0011-2     Document Type: Review

References (117)

1. Amici A, Levine RL, Tsai L, Stadtman ER (1989) Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J Biol Chem 264: 3341-3346
2. Armstrong RC, Swallow AJ (1969) Pulse- and gamma-radiolysis of aqueous solutions of tryptophan. Radiation Res 41: 563-579
3. Armstrong SG, Dean RT (1995) A sensitive fluorometric assay for protein-bound DOPA and related products of radical-mediated protein oxidation. Redox Report 1: 291-298
4. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87: 1620-1624
5. Beckman JS, Ischiropoulos H, Zhu L, van der Woerd M, Smith C, Chen J, Harrison J, Martin JC, Tsai M (1992) Kinetics of superoxide dismutase-and iron-catalyzed nitration of phenolics by peroxynitrite. Arch Biochem Biophys 298: 438-445
6. Berlett BS, Chock PB, Stadtman ER (1990) Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid facilitated dismutation of hydrogen peroxide. Proc Natl Acad Sci USA 87: 389-393
7. Berlett BS, Friguet B, Yim MB, Chock PB, Stadtman ER (1996) Peroxynitrite-mediated nitration of tyrosine residues in Escherichia coli glutamine synthetase mimics adenylylation: relevance to signal transduction. Proc Natl Acad Sci USA 93: 1776-1780
8. Buss H, Chan TP, Sluis KB, Domigan NM, Winterbourn CC (1997) Protein carbonyl measurement by a sensitive ELISA method. Free Rad Biol Med 23: 361-366
9. Candeias LP, Patel KB, Stratford RL, Wardman P (1993) Free hydroxyl radicals are formed between the neutrophil-derived species superoxide and hypochlorous acid. FEBS Lett 333: 151-153
10. Candeias LP, Stratford MRL, Wardman P (1994) Formation of hydroxyl radicals on reaction of hypochlorous acid with ferrocyanide, a model iron(II) complex. Free Rad Res 20: 241-249
11. Cao G, Cutler RG (1995) Protein oxidation and aging. I. Difficulties in measuring reactive protein carbonyls in tissues using 2,4- dinitrophenylhydrazine. Arch Biochem Biophys 320: 106-114
12. Carney JM, Starke-Reed PE, Oliver CN, Landum RW, Cheng MS, Wu JF, Floyd RA (1991) Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-α-phenylnitrone. Proc Natl Acad Sci USA 88: 3633-3636
13. Cerami A, Vlassara H, Brownlee M (1987) Glucose and aging. Sci Am 256: 90-96
14. Ciorba MA. Heinemann SH, Weissbach H, Brot N, Hoshi T (1997) Modulation of potassium channel function by methionine oxidation and reduction. Proc Natl Acad Sci USA 94: 9932-9937
15. Climent I, Tsai L, Levine RL (1990) Derivatization of γ-glutamyl semialdehyde residues in oxidized proteins by fluoresceinamine. Anal Biochem 182: 226-232
16. Creeth JM, Cooper B, Donald ASR, Clamp JR (1983) Studies of the limited degradation of mucous glycoproteins. Biochem J 211: 323-332
17. Culotta E, Koshland DE (1992) NO news is good news. Science 258: 1862-1865
18. Davies KJA (1985) Free radicals and protein degradation in human red blood cells. In: Eaton JW, Konzen DK, White JG (eds) Cellular and molecular aspects of aging: the red cell as a model. Proceedings of a conference held in Minneapolis, MN, 1984, Alan Liss, New York, pp 15-24
19. th international conference on superoxide and superoxide dismutase held in Rome, Italy, 1985, Elsevier, Amsterdam New York Oxford, pp 443-450
20. Davies KJA (1988) Protein oxidation, protein cross-linking, and proteolysis in the formation of lipofuscin: rationale and methods for the measurement of protein degradation. In: Zs-Nagy I (ed) Lipofuscin-1987. Proceedings of an international symposium held in Debrecen, Hungary, on 26-30 August 1987, Elsevier, Amsterdam New York Oxford, pp 109-133
21. Davies KJA, Delsignore ME, Lin SW (1987) Protein damage by oxygen radicals. II. Modification of amino acids. J Biol Chem 262: 9902-9907
22. Dean RT, Geiseg S, Davies MJ (1993) Reactive species and their accumulation on radical-damaged proteins. Trends Biochem Sci 18: 437-441
23. Dean RT, Armstrong S, Fu S, Jessup W (1994) Oxidized proteins and their enzymatic proteolysis in eucaryotic cells: a critical appraisal. In: Nohl H, Esterbauer H, Rice-Evans C (eds) Free radicals in the environment, medicine, and toxicology, Richelieu Press, Londong, pp 47-79
24. Dean RT, Fu S, Stocker R, Davies MJ (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 324: 1-18
25. Farber JM, Levine RL (1986) Sequence of a peptide susceptible to mixed-function oxidation: probable cation binding site in glutamine synthetase. J Biol Chem 261: 4575-4578
26. Folks LK, Candeias LP, Wardman P (1995) Kinetics and mechanisms of hypochlorous acid reactions. Arch Biochem Biophys 323: 120-126
27. Friguet B, Stadtman ER, Szweda LI (1994) Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease. J Biol Chem 269: 21639-21643
28. Fucci L, Oliver CN, Coon MJ, Stadtman ER (1983) Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implications in protein turnover and aging. Proc Natl Acad Sci USA 80: 1521-1525
29. Garner B, Waldeck AR, Witting PK, Rye KA, Stocker R (1998) Oxidation of high density lipoproteins. II. Evidence for direct reduction of lipid hydroperoxides by methionine residues of apolipoproteins AI and AII. J Biol Chem 273: 6088-6095
30. Garrison WM (1987) Reaction mechanisms in radiolysis of peptides, polypeptides, and proteins. Chem Rev 87: 381-398
31. Garrison WM, Jayko ME, Bennett W (1962) Radiation-induced oxidation of protein in aqueous solution. Rad Research 16: 483-502
32. Gieseg SP, Simpson JA, Charlton TS, Duncan MW, Dean RT (1993) Protein-bound 3,4-dehydroxyphenylalanine is a major product formed during hydroxyl radical damage to proteins. Biochemistry 32: 4780-4786
33. Giulivi C, Davies KJA (1993) Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19S) proteasome. J Biol Chem 268: 8752-8759
34. Gow A, Duran D, Thom SR, Ischiropoulos H (1996) Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch Biochem Biophys 333: 42-48
35. Grandhee S, Monnier VM (1991) Mechanism of formation of the Maillard protein cross-link pentosidine. J Biol Chem 266: 11649-11653
36. Grant AJ, Jessup W, Dean RT (1992) Accelerated endocytosis and incomplete catabolism of radical-damaged protein. Biochem Biophys Acta 1134: 203-209
37. Guptasarma P, Balasubramanian D, Matsugo S, Saito I (1992) Hydroxyl radical mediated damage to proteins with special reference to the crystallins. Biochemistry 31: 4296-4302
38. Harrison JE, Schultz J (1976) Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 251: 1371-1374
39. Stadtman ER (1988) Biochemical markers of aging. Exp Gerontol 23: 327-347
40. Hawkins CL, Davies MJ (1998) Hypochlorite-induced damage to proteins: formation of nitrogen-centered radicals from lysine residues and their role in protein fragmentation. Biochem J 332: 617-625
41. Hawkins CL, Davies MJ (1999) Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centered radicals and their role in protein fragmentation. Biochem J 340: 539-548
42. Heinecke JW, Li W, Daehnke HL III, Goldstein JA (1993) Dityrosine, a specific marker of oxidation. J Biol Chem 268: 4069-4077
43. Hensley K, Maidt ML, Pye QN, Stewart CA, Wack M, Tabatabaie T, Floyd RA (1997) Quantitation of protein-bound 3-nitrotyrosine and 3,4- dihydroxyphenylalanine by high-performance liquid chromatography with electrochemical array detection. Anal Biochem 251: 187-195
44. Huggins TG, Wells-Knecht MC, Detorie NA, Baynes JW, Thorpe SR (1993) Formation of o-tyrosine and dityrosine proteins during radiolytic and metal-catalyzed oxidation. J Biol Chem 268: 12341-12347
45. Ignarro L (1989) Endothelium-derived nitric oxide: pharmacology and relationship to the actions of organic esters. Pharm Res 6: 651-659
46. Ischiropoulos H, Al-Medi AB (1995) Peroxynitrite-mediated oxidative protein modifications. FEBS Lett 364: 279-282
47. Keller RJ, Halmes NC, Hinson JA, Pumford NR (1993) Immunochemical detection of oxidized proteins. Chem Res Toxicol 6: 430-433
48. Kettle AJ (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett 379: 103-106
49. Kikugawa K, Kato T, Okamoto Y (1994) Damage of amino acids and proteins induced by nitrogen dioxide, a free radical toxin in air. Free Rad Biol Med 16: 373-382
50. 2 peptide. Proc Natl Acad Sci USA 93: 3377-3382
51. Kopoldova J, Liebster J (1963) The mechanism of radiation chemical degradation of amino acids. Int J Appl Radial Isotopes 14: 493-498
52. Lavine TF (1947) The formation, resolution, and optical properties of the diasteriomeric sulfoxides derived from L-methionine. J Biol Chem 169: 477-491
53. Lee AT, Cerami A (1990) Modification of proteins and nucleic acids by reducing sugars: possible role in aging. In: Schneider EL, Rowe JW (eds) Handbook of the biology of aging, 3rd edn. Academic Press, New York, pp 116-130
54. Lenz AG, Costabel U, Shaltiel S, Levine RL (1989) Determination of carbonyl groups of oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal Biochem 177: 419-425
55. Levine RL (1983) Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system. J Biol Chem 258: 11828-11833
56. Levine RL (1989) Proteolysis induced by metal-catalyzed oxidation. Cell Biol Rev 21: 347-360
57. Levine RL (2002) Carbonyl modified proteins in cellular regulation, aging, and disease. Free Rad Biol Med 32: 790-796
58. Levine RL, Oliver CN, Fulks RM, Stadtman ER (1981) Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis. Proc Natl Acad Sci USA 78: 2120-2124
59. Levine RL, Garland D, Oliver CN, Amici A, Climent I, Lens AG, Ahn BW, Shaltiel S, Stadtman ER (1990) Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 186: 464-478
60. Levine RL, Mosoni L, Berlett BS, Stadtman ER (1996) Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci USA 93: 15036-15040
61. Levine RL, Moskovitz J, Stadtman ER (2000a) Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 50: 301-307
62. Levine RL, Wehr N, Williams JA, Stadtman ER, Shacter E (2000b) Determination of carbonyl groups in oxidized proteins. Methods Mol Biol 99: 15-24
63. Li J, Billiar TR, Talanian RV, Kim YM (1997) Nitric oxide reversibly inhibits seven members of the caspase family via S-nitrosylation. Biochem Biophys Res Commun 240: 419-424
64. Maier KL, Matejkova E, Hinze H, Leuschel L, Weber H, Beck-Speier I (1989) Different selectivities of oxidants during oxidation of methionine residues of the α-1 proteinase inhibitor. FEBS Lett 250: 221-226
65. Mannick JB, Hausladen A, Liu L, Hess DT, Zeng M, Miao QX, Kane LS, Gow AJ, Stamler JS (1998) Fas-induced caspase denitrosylation. Science 284: 651-654
66. Maskos Z, Rush JD, Koppenol WH (1992) The hydroxylation of phenylalanine and tyrosine: a comparison with salicylate and tryptophan. Arch Biochem Biophys 296: 521-529
67. Mohr S, Zech B, Lapetina EG, Brüne B (1987) Inhibition of caspase-3 by s-nitrosation and oxidation caused by nitric oxide. Biochem Biophys Res Commun 238: 387-391
68. Moncada S, Palmer RMJ, Higgs EA (1991) Nitric oxide: physiology, pathophysiology, and pharmacology. Pharm Rev 43: 109-142
69. Nakao LS, Ouchi D, Agusto O (1999) Oxidation of acetaldehyde by peroxynitrite and hydrogen peroxide/iron (II). Production of acetate, formate, and methyl radicals. Chem Res Toxicol 12: 1010-1018
70. Oliver CN, Levine RL, Stadtman ER (1981) Regulation of glutamine synthetase degradation. In: Holzer H (ed) Proceedings of the international conference on metabolic interconversion of enzymes, Titisee, Germany, 1980, Springer, Berlin Heidelberg New York, pp 259-267
71. Oliver CN, Levine RL, Stadtman ER (1987) A role of mixed-function oxidation reactions in the accumulation of altered enzyme forms during aging. J Am Geriatric Soc 35: 947-956
72. Peskin AV, Winterbourn CC (2001) Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Rad Biol Med 30: 572-579
73. Poston JM (1988) Detection of oxidized amino acid residues using P-aminobenzoic acid adducts. Fed Proc 46: 1979 (abstract)
74. Pryor WA, Squadrito GL (1995) The chemistry of peroxynitrite: a product of the reaction of nitric oxide with superoxide. Am J Physiol 268: L699-L722
75. Radi R, Beckman JS, Bush KM, Freeman BA (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 266: 4244-4250
76. 2macroglobulin tetramers into dysfunctional dimers. J Biol Chem 269: 4683-4691
77. Requena JR, Fu MX, Ahmed MU, Jenkins AJ, Lyons TG, Thorpe SR (1996) Lipoxidation products as biomarkers of oxidative damage to proteins during lipid peroxidation reactions. Nephrol Dial Transplant 11 [Suppl 5]: 48-53
78. Requena JR, Chao C-C, Levine RL, Stadtman ER (2001) Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc Natl Acad Sci USA 98: 69-74
79. Rivett AJ (1986) Regulation of intracellular protein turnover: covalent modification as a mechanism of marking proteins for degradation. Curr Top Cell Regul 28: 291-337
80. Rivett AJ, Roseman JE, Oliver CN, Levine RL, Stadtman ER (1985) Covalent modification of proteins by mixed-function oxidation: recognition by intracellular proteases. In: Khairallah EA, Bond JS, Bird JWC (eds) Intracellular protein catabolism. Alan R Liss, New York, pp 317-328
81. Robinson CE, Keshavorzian A, Pasco DS, Frommel TO, Winslip DH, Holmes EW (1999) Determination of protein carbonyl groups by immoblotting. Anal Biochem 266: 48-57
82. Rubbo H, Denicola A, Radi R (1994) Peroxynitrite inactivates thiol-containing enzymes of Trypanosome crigi energetic metabolism and inhibits cell respiration. Arch Biochem Biophys 3808: 96-102
83. Samuni A, Aronovitch J, Godinger D, Chevion M, Czapski G (1983) On the cytotoxicity of vitamin C and metal ions: a site-specific Fenton mechanism. Eur J Biochem 137: 119-124
84. Saxena AK, Saxena P, Wu X, Obrenovich M, Weiss MF, Monnier VM (1999) Biochem Biophys Res Commun 260: 332-338
85. Schuessler H, Schilling K (1984) Oxygen effect in radiolysis of proteins. Part 2. Bovine serum albumin. Int J Radiat Biol 45: 267-281
86. Shacter E, Williams JA, Lim M, Levine RL (1994) Differential susceptibility of plasma proteins to oxidative modification. Examination by Western blot immunoassay. Free Rad Biol Med 17: 429-437
87. Sigalov AB, Stern LJ (1998) Enzymatic repair of oxidative damage to human apolipoprotein A-I. FEBS Lett 433: 196-200
88. Smith MA, Sayre LM, Anderson VE, Harris PL, Beal MF, Kowall N, Perry G, Richey HP, Beckman JS, Rudnicka-Nawrot M, Richey PL, Praprotnik D, Mulvihill P, Miller CA, Cras P, Siedlak SL (1998) Cytochemical demonstration of oxidative damage in Alzheimer's disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J Histochem Cytochem 46: 731-735
89. Squadrito GL, Pryor WA (1998) Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide. Free Rad Biol Med 25: 392-403
90. Stadtman ER (1988) Protein modification in aging. J Gerontol: Biol Sci 43: B112-B120
91. Stadtman ER (1990) Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Rad Biol Med 9: 315-325
92. Stadtman ER, Berlett BS (1989) Fenton chemistry revisited. In: Simic MG, Taylor KA, Ward JF, von Sonntag C (eds) Oxygenradicals in biology and medicine. Plenum Publishers Group, New York, pp 131-136
93. Stadtman ER, Berlett BS (1991) Fenton chemistry: amino acid oxidation. J Biol Chem 266: 17201-17211
94. Stadtman ER, Berlett BS, Chock PB (1990) Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer. Proc Natl Acad Sci USA 87: 384-388
95. Stadtman ER, Starke-Reed PE, Oliver CN, Camey JM, Floyd RA (1992) Protein modification in aging. In: Emerit I, Chance B (eds) Free radicals in aging. Proceedings of an international conference, Paris, 1991. Birkhauser, Basel Boston Berlin, pp 64-72
96. Stamler JS (1994) Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78: 931-936
97. Starke-Reed PE, Oliver CN (1989) Protein oxidation and proteolysis during aging and oxidative stress. Arch Biochem Biophys 275: 559-567
98. Stubauer G, Giuffre A, Sarti P (1999) Mechanism of S-nitrosothiol formation and degradation mediated by copper ions. J Biol Chem 274: 28128-28133
99. Swallow AJ (1960) Effect of ionizing radiation on proteins, RCO groups, peptide bond cleavage, inactivation, -SH oxidation. In: Swallow AJ (ed) Radiation chemistry of organic compounds. John Wiley & Sons, New York, pp 211-224
100. Taborsky G (1973) Oxidative modification of proteins in the presence of ferrous iron and air. Biochem 12: 1341-1348
101. Tien M, Berlett BS, Levine RL, Chock PB, Stadtman ER (1999) Peroxynitrite-mediated modification of protein at physiological carbon dioxide concentrations: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation. Proc Natl Acad Sci USA 96: 7809-7814
102. Uchida K, Kawakishi S (1993) 2-oxohistidine as a novel biological marker for oxidatively modified proteins. FEBS Lett 332: 208-210
103. Uchida K, Stadtman ER (1993) Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 268: 6388-6393
104. Uchida K, Kato Y, Kawakishi S (1990) A novel mechanism for oxidative damage of prolyl peptides induced by hydroxyl radicals. Biochem Biophys Res Commun 169: 265-271
105. Uppu RM, Lemercier J-N, Squadrito GL, Zhang H, Bolzan RM, Pryor WA (1998) Nitrosation by peroxynitrite: use of phenol as a probe. Arch Biochem Biophys 358: 1-16
106. van der Vliet A, Eiserich JP, O'Neill CA, Halliwell B, Cross CE (1995) Tyrosine modification by reactive oxygen species. A closer look. Arch Biochem Biophys 319: 341-349
107. Verzijl N, De Groot J, Oldehinkel E, Bank RA, Thorpe SR, Baynes JW, Bayliss MT, Bijlsma WJ, Lafeber FPJG, Tekoppele JM (2000) Age accumulation of Maillard products in human articular cartilage collagen. Biochem J 350: 381-387
108. Vissers MC, Winterbourn CC (1991) Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl. Arch Biochem Biophys 285: 53-59
109. Viner RI, Williams TD, Schoeneich C (1999) Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca ATPase. Biochemistry 38: 12408-12415
110. Vogt W (1995) Oxidation of methionine residues in proteins: tools, targets, and reversal. Free Rad Biol Med 18: 93-105
111. Wells-Knecht MC, Huggins TG, Dyer SR, Thorpe SR, Baynes JW (1993) Oxidized amino acids in lens protein with age. Measurement of o-tyrosine and dityrosine in the aging human lens. J Biol Chem 269: 12348-12353
112. Wells-Knecht KJ, Zyzak DV, Litchfield JE, Thorpe SR, Baynes JW (1995) Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 34: 3702-3709
113. Winchester RV, Lynn KR (1970) X- and γ-radiolysis of some tryptophan dipeptides. Int Radiat Biol 17: 541-549
114. Wink DA, Mitchell JB (1998) Chemical biology of nitric oxide: insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide. Free Rad Biol Med 25: 434-456
115. Wolf SP, Garner A, Dean RT (1986) Free radicals, lipids, and protein degradation. Trends Biochem Sci 11: 1-5
116. Yim MB, Berlett BS, Chock PB, Stadtman ER (1990) Manganese(II)- bicarbonate-mediated catalytic activity for hydrogen peroxide dismutation and amino acid oxidation: detection of free radical intermediates. Proc Natl Acad Sci USA 87: 394-398
117. Zhang Y-Y, Xu A-M, Noman M, Walsh M, Keaney JF Jr (1996) Nitrosation of tryptophan residue(s) in serum albumin and model peptides. J Biol Chem 271: 14271-14279