Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention

Journal of Clinical Biochemistry and Nutrition

Volumn 48, Issue 1, 2011, Pages 8-19

  Davies, Michael J ^a,b  

^a HEART RESEARCH INSTITUTE   (Australia)

^b University of Sydney   (Australia)

Author keywords

Chloramines; Hypochlorous acid; Myeloperoxidase; Neutrophil; Protein oxidation

Indexed keywords

ALDEHYDE; BROMAMINE; CERULOPLASMIN; CHLORAMINE DERIVATIVE; CYANIC ACID; HYDRAZIDE; HYDRAZINE; HYDROGEN PEROXIDE; HYDROPEROXIDE; HYPOBROMOUS ACID; HYPOCHLOROUS ACID; HYPOTHIOCYANOUS ACID; MYELOPEROXIDASE; NITRIC OXIDE; NITRITE; PEROXIDASE; PEROXYNITRITE; RADICAL; SUPEROXIDE; UNCLASSIFIED DRUG;

CATALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HALOGENATION; HUMAN; LEUKOCYTE ACTIVATION; REVIEW;

MAMMALIA;

EID: 78650750400     PISSN: 09120009     EISSN: None     Source Type: Journal    
DOI: 10.3164/jcbn.11-006FR     Document Type: Review

References (227)

1. Babior BM. The respiratory burst oxidase. TIBS 1987; 12: 241-243.
2. Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem 1995; 64: 97-112.
3. Babior BM. Phagocytes and oxidative stress. Am J Med 2000; 109: 33-44.
4. Schultz J, Kaminker K. Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization. Arch Biochem Biophys 1962; 96: 465-467.
5. Daugherty A, Dunn JL, Rateri DL, Heinecke JW. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J Clin Invest 1994; 94: 437-444.
6. 2/halide system in human atherosclerotic lesions - Colocalization of myeloperoxidase and hypochlorite-modified proteins. Eur J Biochem 2000; 267: 4495-4503.
7. Nauseef WM. Myeloperoxidase deficiency. Hematol Oncol Clin North Am 1988; 2: 135-158.
8. Kutter D, Devaquet P, Vanderstocken G, Paulus JM, Marchal V, Gothot A. Consequences of total and subtotal myeloperoxidase deficiency: risk or benefit? Acta Haematol 2000; 104: 10-15.
9. Klebanoff SJ. Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J Bacteriol 1968; 95: 2131-2138.
10. Davies MJ, Hawkins CL, Pattison DI, Rees MD. Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid Redox Signal 2008; 10: 1199-1234.
11. Kettle AJ, Winterbourn CC. Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep 1997; 3: 3-15.
12. van der Veen BS, de Winther MP, Heeringa P. Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease. Antioxid Redox Signal 2009; 11: 2899-2937.
13. Fiedler TJ, Davey CA, Fenna RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem 2000; 275: 11964-11971.
14. Zeng J, Fenna RE. X-ray crystal structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 1992; 226: 185-207.
15. Bolscher BG, Wever R. A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate. Biochim Biophys Acta 1984; 788: 1-10.
16. Furtmüller PG, Zederbauer M, Jantschko W, and et al. Active site structure and catalytic mechanisms of human peroxidases. Arch Biochem Biophys 2006; 445: 199-213.
17. Abu-Ghazaleh RI, Dunnette SL, Loegering DA, and et al. Eosinophil granule proteins in peripheral blood granulocytes. J Leukoc Biol 1992; 52: 611-618.
18. Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ. Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J Exp Med 1989; 169: 1757-1769.
19. Ihalin R, Loimaranta V, Tenovuo J. Origin, structure, and biological activities of peroxidases in human saliva. Arch Biochem Biophys 2006; 445: 261-268.
20. Ueda T, Sakamaki K, Kuroki T, Yano I, Nagata S. Molecular cloning and characterization of the chromosomal gene for human lactoperoxidase. Eur J Biochem 1997; 243: 32-41.
21. Miyasaki KT, Zambon JJ, Jones CA, Wilson ME. Role of high avidity binding of human neutrophil myeloperoxidase in the killing of Actinobacillus actinomycetemcomitans. Infect Immun 1987; 55: 1029-1036.
22. 2-Cl-system. J Infect Dis 1978; 137: 481-485.
23. Ramsey PG, Martin T, Chi E, Klebanoff SJ. Arming of mononuclear phagocytes by eosinophil peroxidase bound to Staphylococcus aureus. J Immunol 1982; 128: 415-420.
24. Baldus S, Eiserich JP, Mani A, and et al. Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration. J Clin Invest 2001; 108: 1759-1770.
25. Astern JM, Pendergraft WF, Falk RJ, and et al. Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma kallikrein-kinin system. Am J Pathol 2007; 171: 349-360.
26. Kubala L, Baldus S, Eiserich JP. Glycosaminoglycan-dependent sequestration of myeloperoxidase within extracellular matrix. Free Radic Biol Med 2004; 37 (Suppl. 1): S52.
27. Rees MD, Whitelock JM, Malle E, and et al. Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan. Matrix Biol 2010; 29: 63-73.
28. Daphna EM, Michaela S, Eynat P, Irit A, Rimon S. Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme. Mol Cell Biochem 1998; 183: 55-61.
29. Green SP, Baker MS, Lowther DA. Depolymerization of synovial fluid hyaluronic acid (HA) by the complete myeloperoxidase (MPO) system may involve the formation of a HA-MPO ionic complex. J Rheumatol 1990; 17: 1670-1675.
30. Tiruppathi C, Naqvi T, Wu Y, Vogel SM, Minshall RD, Malik AB. Albumin mediates the transcytosis of myeloperoxidase by means of caveolae in endothelial cells. Proc Natl Acad Sci USA 2004; 101: 7699-7704.
31. Segelmark M, Persson B, Hellmark T, Wieslander J. Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin? Clin Exp Immunol 1997; 108: 167-174.
32. Bouriche H, Salavei P, Lessig J, Arnhold J. Differential effects of flavonols on inactivation of alpha1-antitrypsin induced by hypohalous acids and the myeloperoxidase-hydrogen peroxide-halide system. Arch Biochem Biophys 2007; 459: 137-142.
33. Zheng L, Nukuna B, Brennan ML, and et al. Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J Clin Invest 2004; 114: 529-541. (Pubitemid 39572103)
34. Carr AC, Myzak MC, Stocker R, McCall MR, Frei B. Myeloperoxidase binds to low-density lipoprotein: potential implications for atherosclerosis. FEBS Lett 2000; 487: 176-180. (Pubitemid 32057108)
35. Zederbauer M, Furtmüller PG, Brogioni S, Jakopitsch C, Smulevich G, Obinger C. Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties. Nat Prod Rep 2007; 24: 571-584. (Pubitemid 46848706)
36. Spalteholz H, Panasenko OM, Arnhold J. Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase. Arch Biochem Biophys 2006; 445: 225-234. (Pubitemid 43082215)
37. Marquez LA, Dunford HB. Reaction of compound-III of myeloperoxidase with ascorbic acid. J Biol Chem 1990; 265: 6074-6078. (Pubitemid 20148142)
38. Marquez LA, Dunford HB. Interaction of acetaminophen with myeloperoxidase intermediates: optimum stimulation of enzyme activity. Arch Biochem Biophys 1993; 305: 414-420. (Pubitemid 23282925)
39. Kettle AJ, Anderson RF, Hampton MB, Winterbourn CC. Reactions of superoxide with myeloperoxidase. Biochemistry 2007; 46: 4888-4897.
40. Arnhold J, Monzani E, Furtmüller PG, Zederbauer M, Casella L, Obinger C. Kinetics and thermodynamics of halide and nitrite oxidation by mammalian heme peroxidases. Eur J Inorg Chem 2006; 19: 3801-3811.
41. van Dalen CJ, Whitehouse MW, Winterbourn CC, Kettle AJ. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J 1997; 327: 487-492.
42. Chapman AL, Skaff O, Senthilmohan R, Kettle AJ, Davies MJ. Hypobromous acid and bromamine production by neutrophils and modulation by superoxide. Biochem J 2009; 417: 773-781.
43. van Dalen CJ, Kettle AJ. Substrates and products of eosinophil peroxidase. Biochem J 2001; 358: 233-239.
44. Furtmüler PG, Jantschko W, Regelsberger G, Jakopitsch C, Arnhold J, Obinger C. Reaction of lactoperoxidase compound I with halides and thiocyanate. Biochemistry 2002; 41: 11895-11900.
45. Ashby MT, Carlson AC, Scott MJ. Redox buffering of hypochlorous acid by thiocyanate in physiologic fluids. J Am Chem Soc 2004; 126: 15976-15977.
46. Nagy P, Beal JL, Ashby MT. Thiocyanate is an efficient endogenous scavenger of the phagocytic killing agent hypobromous acid. Chem Res Toxicol 2006; 19: 587-593.
47. Morris JC. The acid ionization constant of HOCl from 5°C to 35°C. J Phys Chem 1966; 70: 3798-3805.
48. Prütz WA, Kissner R, Koppenol WH, Rüegger H. On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids. Arch Biochem Biophys 2000; 380: 181-191. (Pubitemid 30616785)
49. Nagy P, Jameson GN, Winterbourn CC. Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione. Chem Res Toxicol 2009; 22: 1833-1840.
50. Ikeda-Saito M. A study of ligand binding to spleen myeloperoxidase. Biochemistry 1987; 26: 4344-4349.
51. Marquez LA, Dunford HB. Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate. J Biol Chem 1994; 269: 7950-7956. (Pubitemid 24200195)
52. Koelsch M, Mallak R, Graham GG, and et al. Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations. Biochem Pharmacol 2010; 79: 1156-1164.
53. Furtmüller PG, Arnhold J, Jantschko W, Pichler H, Obinger C. Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase. Biochem Biophys Res Commun 2003; 301: 551-557. (Pubitemid 36279276)
54. Furtmüller PG, Arnhold J, Jantschko W, Zederbauer M, Jakopitsch C, Obinger C. Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase. J Inorg Biochem 2005; 99: 1220-1229. (Pubitemid 40503085)
55. Marquez LA, Dunford HB. Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications for lipoprotein peroxidation studies. J Biol Chem 1995; 270: 30434-30440. (Pubitemid 26005098)
56. Bayse GS, Michaels AW, Morrison M. The peroxidase catalyzed oxidation of tyrosine. Biochim Biophys Acta 1972; 284: 34-42.
57. Pattison DI, Davies MJ. Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds. Chem Res Toxicol 2001; 14: 1453-1464.
58. Pattison DI, Davies MJ. Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases. Curr Med Chem 2006; 13: 3271-3290.
59. Pattison DI, Hawkins CL, Davies MJ. Hypochlorous acid-mediated oxidation of lipid components and antioxidants present in low-density lipoproteins: absolute rate constants, product analysis and computational modeling. Chem Res Toxicol 2003; 16: 439-449.
60. Carr AC, Winterbourn CC. Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem J 1997; 327: 275-281. (Pubitemid 27455490)
61. Davies MJ, Hawkins CL. Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates. Free Radic Res 2000; 33: 719-729.
62. Vissers MC, Winterbourn CC. Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid. Biochem J 1995; 307: 57-62.
63. Lloyd MM, van Reyk DM, Davies MJ, Hawkins CL. Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid. Biochem J 2008; 414: 271-280.
64. Hawkins CL, Pattison DI, Davies MJ. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 2003; 25: 259-274. (Pubitemid 38041264)
65. Fu X, Mueller DM, Heinecke JW. Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: a potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase. Biochemistry 2002; 41: 1293-1301. (Pubitemid 34083782)
66. Harwood DT, Kettle AJ, Winterbourn CC. Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method. Biochem J 2006; 399: 161-168.
67. Raftery MJ, Yang Z, Valenzuela SM, Geczy CL. Novel intra- and intermolecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation. J Biol Chem 2001; 276: 33393-33401. (Pubitemid 37384547)
68. Pullar JM, Vissers MC, Winterbourn CC. Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide. J Biol Chem 2001; 276: 22120-22125. (Pubitemid 37410877)
69. Harwood DT, Kettle AJ, Brennan S, Winterbourn CC. Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 2009; 877: 3393-3399.
70. Pullar JM, Winterbourn CC, Vissers MC. Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. Am J Physiol 1999; 277: H1505-H1512.
71. Fu X, Kassim SY, Parks WC, Heinecke JW. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 2001; 276: 41279-41287. (Pubitemid 37373286)
72. Hawkins CL, Davies MJ. Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function. Chem Res Toxicol 2005; 18: 1600-1610.
73. Pattison DI, Hawkins CL, Davies MJ. Hypochlorous acid-mediated protein oxidation: How important are chloramine transfer reactions and protein tertiary structure? Biochemistry 2007; 46: 9853-9864.
74. Kim HY, Gladyshev VN. Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 2007; 407: 321-329.
75. Matheson NR, Travis J. Differential effects of oxidizing agents on human plasma alpha-1-proteinase inhibitor and human neutrophil myeloperoxidase. Biochemistry 1985; 24: 1941-1945. (Pubitemid 15019790)
76. Vissers MC, Winterbourn CC. Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes. Biochem J 1987; 245: 277-280.
77. Khor HK, Fisher MT, Schöneich C. Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO-). J Biol Chem 2004; 279: 19486-19493. (Pubitemid 38623383)
78. Midwinter RG, Cheah FC, Moskovitz J, Vissers MC, Winterbourn CC. IkappaB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-kappaB activity by glycine chloramine through methionine oxidation. Biochem J 2006; 396: 71-78. (Pubitemid 43764498)
79. Thomas EL. Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli. Infect Immun 1979; 23: 522-531.
80. Winterbourn CC. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 1985; 840: 204-210.
81. Thomas EL, Grisham MB, Jefferson MM. Preparation and characterization of chloramines. Method Enzymol 1986; 132: 569-585.
82. Prütz WA. Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates. Arch Biochem Biophys 1996; 332: 110-120.
83. Prütz WA. Interactions of hypochlorous acid with pyrimidine nucleotides, and secondary reactions of chlorinated pyrimidines with GSH, NADH, and other substrates. Arch Biochem Biophys 1998; 349: 183-191.
84. Rees MD, Hawkins CL, Davies MJ. Hypochlorite-mediated fragmentation of hyaluronan, chondritin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactios, and site-specific fragmentation. J Am Chem Soc 2003; 125: 13719-13733.
85. Kawai Y, Kiyokawa H, Kimura Y, Kato Y, Tsuchiya K, Terao J. Hypochlorous acid-derived modification of phospholipids: characterization of aminophospholipids as regulatory molecules for lipid peroxidation. Biochemistry 2006; 45: 14201-14211. (Pubitemid 44846209)
86. Kettle AJ. Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett 1996; 379: 103-106.
87. Winterbourn CC. Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid. Toxicology 2002; 181-182: 223-227.
88. Fu X, Kao JL, Bergt C, and et al. Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specific structural motifs control protein oxidation. J Biol Chem 2004; 279: 6209-6212. (Pubitemid 38248751)
89. Gould JP, Richards JT, Miles MG. The formation of stable organic chloramines during the aqueous chlorination of cytosine and 5-methylcytosine. Water Res 1984; 18: 991-999.
90. Henderson JP, Byun J, Williams MV, and et al. Bromination of deoxycytidine by eosinophil peroxidase: a mechanism for mutagenesis by oxidative damage of nucleotide precursors. Proc Natl Acad Sci USA 2001; 98: 1631-1636. (Pubitemid 32166276)
91. Henderson JP, Byun J, Williams MV, Mueller DM, McCormick ML, Heinecke JW. Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation. J Biol Chem 2001; 276: 7867-7875. (Pubitemid 37385581)
92. Henderson JP, Byun J, Takeshita J, Heinecke JW. Phagocytes produce 5-chlorouracil and 5-bromouracil, two mutagenic products of myeloperoxidase, in human inflammatory tissue. J Biol Chem 2003; 278: 23522-23528. (Pubitemid 36830171)
93. Henderson JP, Byun J, Mueller DM, Heinecke JW. The eosinophil peroxidasehydrogen peroxide-bromide system of human eosinophils generates 5-bromouracil, a mutagenic thymine analogue. Biochemistry 2001; 40: 2052-2059. (Pubitemid 32165674)
94. Masuda M, Suzuki T, Friesen MD, and et al. Chlorination of guanosine and other nucleosides by hypochlorous acid and myeloperoxidase of activated human neutrophils. Catalysis by nicotine and trimethylamine. J Biol Chem 2001; 276: 40486-40496. (Pubitemid 37373187)
95. Chen HJ, Row SW, Hong CL. Detection and quantification of 5-chlorocytosine in DNA by stable isotope dilution and gas chromatography/ negative ion chemical ionization/mass spectrometry. Chem Res Toxicol 2002; 15: 262-268. (Pubitemid 34163807)
96. Whiteman M, Jenner A, Halliwell B. Hypochlorous acid-induced base modifications in isolated calf thymus DNA. Chem Res Toxicol 1997; 10: 1240-1246.
97. Whiteman M, Jenner A, Halliwell B. 8-Chloroadenine: a novel product formed from hypochlorous acid-induced damage to calf thymus DNA. Biomarkers 1999; 4: 303-310.
98. Shen Z, Mitra SN, Wu W, and et al. Eosinophil peroxidase catalyzes bromination of free nucleosides and double-stranded DNA. Biochemistry 2001; 40: 2041-2051.
99. Kawai Y, Morinaga H, Kondo H, and et al. Endogenous formation of novel halogenated 2′-deoxycytidine. Hypohalous acid-mediated DNA modification at the site of inflammation. J Biol Chem 2004; 279: 51241-51249.
100. Takeshita J, Byun J, Nhan TQ, and et al. Myeloperoxidase generates 5-chlorouracil in human atherosclerotic tissue. A potential pathway for somatic mutagenesis by macrophages. J Biol Chem 2006; 281: 3096-3104.
101. van den Berg JJ, Winterbourn CC, Kuypers FA. Hypochlorous acid-mediated modification of cholesterol and phospholipid: analysis of reaction products by gas chromatography-mass spectrometry. J Lipid Res 1993; 34: 2005-2012.
102. Arnhold J, Panasenko OM, Schiller J, Vladimirov Yu A, Arnold K. The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis. Chem Phys Lipids 1995; 78: 55-64.
103. Panasenko OM, Spalteholz H, Schiller J, Arnhold J. Myeloperoxidase- induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines. Free Radic Biol Med 2003; 34: 553-562.
104. Carr AC, van den Berg JJ, Winterbourn CC. Chlorination of cholesterol in cell membranes by hypochlorous acid. Arch Biochem Biophys 1996; 332: 63-69.
105. Carr AC, van den Berg JJ, Winterbourn CC. Differential reactivities of hypochlorous and hypobromous acids with purified Escherichia coli phospholipid: formation of haloamines and halohydrins. Biochim Biophys Acta 1998; 1392: 254-264.
106. Jerlich A, Pitt AR, Schaur RJ, Spickett CM. Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS. Free Radic Biol Med 2000; 28: 673-682.
107. Heinecke JW, Li W, Mueller DM, Bohrer A, Turk J. Cholesterol chlorohydrin synthesis by the myeloperoxidase-hydrogen peroxide-chloride system: potential markers for lipoproteins oxidatively damaged by phagocytes. Biochemistry 1994; 33: 10127-10136.
108. Skaff O, Pattison DI, Davies MJ. The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study. Biochemistry 2008; 47: 8237-8245.
109. Albert CJ, Thukkani AK, Heuertz RM, Slungaard A, Hazen SL, Ford DA. Eosinophil peroxidase-derived reactive brominating species target the vinyl ether bond of plasmalogens generating a novel chemoattractant, alpha-bromo fatty aldehyde. J Biol Chem 2003; 278: 8942-8950.
110. Thukkani AK, Albert CJ, Wildsmith KR, and et al. Myeloperoxidase-derived reactive chlorinating species from human monocytes target plasmalogens in low density lipoprotein. J Biol Chem 2003; 278: 36365-36372.
111. Thukkani AK, McHowat J, Hsu FF, Brennan ML, Hazen SL, Ford DA. Identification of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions. Circulation 2003; 108: 3128-3133.
112. Pattison DI, Davies MJ. Kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and the use of 3-bromotyrosine as a marker of oxidative stress. Biochemistry 2004; 43: 4799-4809.
113. Skaff O, Pattison DI, Davies MJ. Kinetics of hypobromous acid-mediated oxidation of lipid components and antioxidants. Chem Res Toxicol 2007; 20: 1980-1988.
114. Vissers MC, Carr AC, Chapman AL. Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis. Biochem J 1998; 330: 131-138.
115. Hawkins CL. The role of hypothiocyanous acid (HOSCN) in biological systems. Free Rad Res 2009; 43: 1147-1158.
116. Saloojee Y, Vesey CJ, Cole PV, Russell MA. Carboxyhaemoglobin and plasma thiocyanate: complementary indicators of smoking behaviour? Thorax 1982; 37: 521-525.
117. Wang Z, Nicholls SJ, Rodriguez ER, and et al. Protein carbamylation links inflammation, smoking, uremia and atherogenesis. Nat Med 2007; 13: 1176-1184.
118. Pattison DI, Hawkins CL, Davies MJ. What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chem Res Toxicol 2009; 22: 807-817.
119. Skaff O, Pattison DI, Davies MJ. Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: Absolute rate constants and assessment of biological relevance. Biochem J 2009; 422: 111-117.
120. Hawkins CL, Pattison DI, Stanley NR, Davies MJ. Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation. Biochem J 2008; 416: 441-452.
121. Aune TM, Thomas EL, Morrison M. Lactoperoxidase-catalyzed incorporation of thiocyanate ion into a protein substrate. Biochemistry 1977; 16: 4611-4615.
122. Lane AE, Tan JT, Hawkins CL, Heather AK, Davies MJ. The myeloperoxidase- derived oxidant HOSCN inhibits protein tyrosine phosphatases and modulates cell signalling via the mitogen-activated protein kinase (MAPK) pathway in macrophages. Biochem J 2010; 430: 161-169.
123. Exner M, Hermann M, Hofbauer R, Hartmann B, Kapiotis S, Gmeiner B. Thiocyanate catalyzes myeloperoxidase-initiated lipid oxidation in LDL. Free Radic Biol Med 2004; 37: 146-155.
124. Kettle AJ, Winterbourn CC. Oxidation of hydroquinone by myeloperoxidase. Mechanism of stimulation by benzoquinone. J Biol Chem 1992; 267: 8319-8324.
125. Burner U, Krapfenbauer G, Furtmüler PG, Regelsberger G, Obinger C. Oxidation of hydroquinone, 2,3-dimethylhydroquinone and 2,3,5- trimethylhydroquinone by human myeloperoxidase. Redox Rep 2000; 5: 185-190.
126. Kettle AJ, Robertson IG, Palmer BD, Anderson RF, Patel KB, Winterbourn CC. Oxidative metabolism of amsacrine by the neutrophil enzyme Myeloperoxidase. Biochem Pharmacol 1992; 44: 1731-1738.
127. van der Walt BJ, van Zyl JM, Kriegler A. Aromatic hydroxylation during the myeloperoxidase-oxidase oxidation of hydrazines. Biochem Pharmacol 1994; 47: 1039-1046.
128. Kettle AJ, Geyde CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic hydrazide. Biochem J 1997; 321: 503-508.
129. Siraki AG, Bonini MG, Jiang J, Ehrenshaft M, Mason RP. Aminoglutethimide-induced protein free radical formation on myeloperoxidase: a potential mechanism of agranulocytosis. Chem Res Toxicol 2007; 20: 1038-1045.
130. Colas C, Ortiz de Montellano PR. Autocatalytic radical reactions in physiological prosthetic heme modification. Chem Rev 2003; 103: 2305-2332.
131. Colas C, De Montellano PR. Horseradish peroxidase mutants that autocatalytically modify their prosthetic heme group: insights into mammalian peroxidase heme-protein covalent bonds. J Biol Chem 2004; 279: 24131-24140.
132. Savenkova ML, Mueller DM, Heinecke JW. Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid-peroxidation in low density lipoprotein. J Biol Chem 1994; 269: 20394-20400.
133. Kapiotis S, Sengoelge G, Hermann M, Held I, Seelos C, Gmeiner BM. Paracetamol catalyzes myeloperoxidase-initiated lipid oxidation in LDL. Arterioscler Thromb Vasc Biol 1997; 17: 2855-2860.
134. Heinecke JW, Li W, Francis GA, Goldstein JA. Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins. J Clin Invest 1993; 91: 2866-2872.
135. Bessems JG, Vermeulen NP. Paracetamol (acetaminophen)-induced toxicity: Molecular and biochemical mechanisms, analogues and protective approaches. Crit Rev Toxicol 2001; 31: 55-138.
136. O'Brien P. Peroxidases. Chem Biol Interact 2000; 129: 113-139.
137. Tafazoli S, O'Brien PJ. Peroxidases: a role in the metabolism and side effects of drugs. Drug Discov Today 2005; 10: 617-625.
138. Grisham MB, Jefferson MM, Thomas EL. Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils. J Biol Chem 1984; 259: 6757-6765.
139. Peskin AV, Midwinter RG, Harwood DT, Winterbourn CC. Chlorine transfer between glycine, taurine and histamine: reaction rates and impact on cellular reactivity. Free Radic Biol Med 2004; 37: 1622-1630.
140. Peskin AV, Winterbourn CC. Histamine chloramine reactivity with thiol compounds, ascorbate and methionine and with intracellular glutathione. Free Radic Biol Med 2003; 35: 1252-1260.
141. Peskin AV, Winterbourn CC. Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase. Free Radic Biol Med 2006; 40: 45-53.
142. Thomas EL, Grisham MB, Jefferson MM. Cytotoxicity of chloramines. Method Enzymol 1986; 132: 585-593.
143. Thomas EL, Bozeman PM, Jefferson MM, King CC. Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines. J Biol Chem 1995; 270: 2906-2913.
144. Pattison DI, Davies MJ. Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation. Biochemistry 2005; 44: 7378-7387.
145. Pattison DI, Davies MJ. Evidence for rapid inter- and intra-molecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous acid mediated damage. Biochemistry 2006; 45: 8152-8162.
146. Hawkins CL, Davies MJ. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem J 1998; 332: 617-625.
147. Hawkins CL, Davies MJ. Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation. Biochem J 1999; 340: 539-548.
148. Armesto XL, Canle ML, Garcia MV, Santaballa JA. Aqueous chemistry of N-halo-compounds. Chem Soc Rev 1998; 27: 453-460.
149. Hazen SL, Gaut JP, Hsu FF, Crowley JR, d'Avignon A, Heinecke JW. p-Hydroxyphenylacetaldehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues. J Biol Chem 1997; 272: 16990-16998.
150. - system. Eur J Biochem 1978; 92: 301-308.
151. Hawkins CL, Davies MJ. The role of aromatic amino acid oxidation, protein unfolding, and aggregation in the hypobromous acid-induced inactivation of trypsin inhibitor and lysozyme. Chem Res Toxicol 2005; 18: 1669-1677.
152. Senthilmohan R, Kettle AJ. Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch Biochem Biophys 2006; 445: 235-244. (Pubitemid 43082216)
153. Pennathur S, Heinecke JW. Mechanisms for oxidative stress in diabetic cardiovascular disease. Antioxid Redox Signal 2007; 9: 955-969. (Pubitemid 46919596)
154. Rees MD, Davies MJ. Heparan sulfate degradation via reductive homolysis of its N-Chloro derivatives. J Am Chem Soc 2006; 128: 3085-3097.
155. Rees MD, Hawkins CL, Davies MJ. Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondritin sulphates. Biochem J 2004; 381: 175-184.
156. Peskin AV, Winterbourn CC. Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radic Biol Med 2001; 30: 572-579.
157. Vissers MC, Lee WG, Hampton MB. Regulation of apoptosis by vitamin C. Specific protection of the apoptotic machinery against exposure to chlorinated oxidants. J Biol Chem 2001; 276: 46835-46840. (Pubitemid 37373051)
158. Test ST, Lampert MB, Ossanna PJ, Thoene JG, Weiss SJ. Generation of nitrogen-chlorine oxidants by human phagocytes. J Clin Invest 1984; 74: 1341-1349.
159. Winterbourn CC, Pichorner H, Kettle AJ. Myeloperoxidase-dependent generation of a tyrosine peroxide by neutrophils. Arch Biochem Biophys 1997; 338: 15-21. (Pubitemid 27200288)
160. Winterbourn CC, Parsons-Mair HN, Gebicki S, Gebicki JM, Davies MJ. Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. Biochem J 2004; 381: 241-248. (Pubitemid 38932230)
161. Das AB, Nagy P, Abbott HF, Winterbourn CC, Kettle AJ. Reactions of superoxide with the myoglobin tyrosyl radical. Free Radic Biol Med 2010; 48: 1540-1547.
162. Nagy P, Kettle AJ, Winterbourn CC. Superoxide-mediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer. J Biol Chem 2009; 284: 14723-14733.
163. Nagy P, Kettle AJ, Winterbourn CC. Neutrophil-mediated oxidation of enkephalins via myeloperoxidase-dependent addition of superoxide. Free Radic Biol Med 2010; 49: 792-799.
164. Ximenes VF, Silva SO, Rodrigues MR, and et al. Superoxide-dependent oxidation of melatonin by myeloperoxidase. J Biol Chem 2005; 280: 38160-38169.
165. Ximenes VF, Maghzal GJ, Turner R, Kato Y, Winterbourn CC, Kettle AJ. Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione. Biochem J 2009; 425: 285-293.
166. Davies MJ, Fu S, Dean RT. Protein hydroperoxides can give rise to reactive free radicals. Biochem J 1995; 305: 643-649.
167. Davies MJ. Reactive species formed on proteins exposed to singlet oxygen. Photochem Photobiol Sci 2004; 3: 17-25.
168. Davies MJ. The oxidative environment and protein damage. Biochim Biophys Acta 2005; 1703: 93-109.
169. Rahmanto AS, Morgan PE, Hawkins CL, Davies MJ. Cellular effects of peptide and protein hydroperoxides. Free Radic Biol Med 2010; 48: 1071-1078.
170. Zgliczyński JM, Stelmaszyńska T, Domański J, Ostrowski W. Chloramines as intermediates of oxidation reaction of amino acids by myeloperoxidase. Biochim Biophys Acta 1971; 235: 419-424.
171. Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW. Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidise α-amino-acids to a family of reactive aldehydes. J Biol Chem 1998; 273: 4997-5005.
172. Hazen SL, Gaut JP, Crowley JR, Hsu FF, Heinecke JW. Elevated levels of protein-bound p-hydroxyphenylacetaldehyde, an amino- acid-derived aldehyde generated by myeloperoxidase, are present in human fatty streaks, intermediate lesions and advanced atherosclerotic lesions. Biochem J 2000; 352: 693-699.
173. Baynes JW. The Maillard hypothesis on aging: time to focus on DNA. Ann N Y Acad Sci 2002; 959: 360-367.
174. Lentner C, ed. Geigy Scientific Tables vol. 3: Physical Chemistry, Composition of Blood, Hematology, Somatometric Data. Basle: Ciba-Geigy Ltd, 1984.
175. Arlandson M, Decker T, Roongta VA, and et al. Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J Biol Chem 2001; 276: 215-224. (Pubitemid 32050310)
176. Kettle AJ, Winterbourn CC. A kinetic analysis of the catalase activity of myeloperoxidase. Biochemistry 2001; 40: 10204-10212.
177. Jantschko W, Furtmüller PG, Zederbauer M, Lanz M, Jakopitsch C, Obinger C. Direct conversion of ferrous myeloperoxidase to compound II by hydrogen peroxide: an anaerobic stopped-flow study. Biochem Biophys Res Commun 2003; 312: 292-298. (Pubitemid 37445171)
178. Winterbourn CC, Hampton MB, Livesey JH, Kettle AJ. Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing. J Biol Chem 2006; 281: 39860-39869.
179. Kettle AJ, Winterbourn CC. Superoxide enhances hypochlorous acid production by stimulated human neutrophils. Biochim Biophys Acta 1990; 1052: 379-385. (Pubitemid 20168845)
180. Kettle AJ, Winterbourn CC. Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid. Biochem J 1988; 252: 529-536.
181. Kettle AJ, Gedye CA, Winterbourn CC. Superoxide is an antagonist of antiinflammatory drugs that inhibit hypochlorous acid production by myeloperoxidase. Biochem Pharmacol 1993; 45: 2003-2010.
182. Subrahmanyam VV, Kolachana P, Smith MT. Hydroxylation of phenol to hydroquinone catalyzed by a human myeloperoxidase-superoxide complex: possible implications in benzene-induced myelotoxicity. Free Radic Res Commun 1991; 15: 285-296.
183. Kettle AJ, Winterbourn CC. Superoxide-dependent hydroxylation by myeloperoxidase. J Biol Chem 1994; 269: 17146-17151.
184. Abu-Soud HM, Hazen SL. Nitric oxide is a physiological substrate for mammalian peroxidases. J Biol Chem 2000; 275: 37524-37532. (Pubitemid 32004861)
185. Lakshmi VM, Nauseef WM, Zenser TV. Myeloperoxidase potentiates nitric oxide-mediated nitrosation. J Biol Chem 2005; 280: 1746-1753.
186. Abu-Soud HM, Hazen SL. Nitric oxide modulates the catalytic activity of myeloperoxidase. J Biol Chem 2000; 275: 5425-5430. (Pubitemid 30115174)
187. Galijasevic S, Saed GM, Hazen SL, Abu-Soud HM. Myeloperoxidase metabolizes thiocyanate in a reaction driven by nitric oxide. Biochemistry 2006; 45: 1255-1262. (Pubitemid 43167192)
188. Galijasevic S, Proteasa G, Abdulhamid I, Abu-Soud HM. The potential role of nitric oxide in substrate switching in eosinophil peroxidase. Biochemistry 2007; 46: 406-415. (Pubitemid 46105433)
189. Eiserich JP, Baldus S, Brennan ML, and et al. Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science 2002; 296: 2391-2394.
190. Grubina R, Huang Z, Shiva S, and et al. Concerted nitric oxide formation and release from the simultaneous reactions of nitrite with deoxy- and oxyhemoglobin. J Biol Chem 2007; 282: 12916-12927. (Pubitemid 47100601)
191. Burner U, Furtmüller PG, Kettle AJ, Koppenol WH, Obinger C. Mechanism of reaction of myeloperoxidase with nitrite. J Biol Chem 2000; 275: 20597-20601.
192. van Dalen CJ, Winterbourn CC, Senthilmohan R, Kettle AJ. Nitrite as a substrate and inhibitor of myeloperoxidase. Implications for nitration and hypochlorous acid production at sites of inflammation. J Biol Chem 2000; 275: 11638-11644. (Pubitemid 30237723)
193. Brennan ML, Wu W, Fu X, and et al. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 2002; 277: 17415-17427.
194. Monzani E, Roncone R, Galliano M, Koppenol WH, Casella L. Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide. Eur J Biochem 2004; 271: 895-906.
195. Sampson JB, Rosen H, Beckman JS. Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase. Methods Enzymol 1996; 269: 210-218. (Pubitemid 26295710)
196. Floris R, Piersma SR, Yang G, Jones P, Wever R. Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase. Eur J Biochem 1993; 215: 767-775. (Pubitemid 23246850)
197. Furtmüller PG, Jantschko W, Zederbauer M, and et al. Peroxynitrite efficiently mediates the interconversion of redox intermediates of myeloperoxidase. Biochem Biophys Res Commun 2005; 337: 944-954. (Pubitemid 41447005)
198. Zhang C, Yang J, Jacobs JD, Jennings LK. Interaction of myeloperoxidase with vascular NAD(P)H oxidase-derived reactive oxygen species in vasculature: implications for vascular diseases. Am J Physiol Heart Circ Physiol 2003; 285: H2563-H2572. (Pubitemid 37443074)
199. Zhang C, Yang J, Jennings LK. Leukocyte-derived myeloperoxidase amplifies high-glucose-induced endothelial dysfunction through interaction with high-glucose-stimulated, vascular non-leukocyte-derived reactive oxygen species. Diabetes 2004; 53: 2950-2959. (Pubitemid 39425921)
200. Dusting GJ, Tan CSW, Jiang F, and et al. Potent inhibitors of vascular oxidative stress: Specific block of Nox4-type NADPH oxidase for cardiovascular and neurological disease. Acta Pharmacol Sin 2006; 27: 3.
201. Dusting GJ, Selemidis S, Jiang F. Mechanisms for suppressing NADPH oxidase in the vascular wall. Mem Inst Oswaldo Cruz 2005; 100: 97-103. (Pubitemid 40685446)
202. Hampton MB, Winterbourn CC. Modification of neutrophil oxidant production with diphenyleneiodonium and its effect on bacterial killing. Free Radic Biol Med 1995; 18: 633-639.
203. Ellis JA, Mayer SJ, Jones OT. The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils. Biochem J 1988; 251: 887-891.
204. Li Y, Trush MA. Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production. Biochem Biophys Res Commun 1998; 253: 295-299. (Pubitemid 29026697)
205. Selemidis S, Dusting GJ, Peshavariya H, Kemp-Harper BK, Drummond GR. Nitric oxide suppresses NADPH oxidase-dependent superoxide production by S-nitrosylation in human endothelial cells. Cardiovasc Res 2007; 75: 349-358. (Pubitemid 46961925)
206. Radi R. Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci USA 2004; 101: 4003-4008. (Pubitemid 38405874)
207. Park YS, Suzuki K, Mumby S, Taniguchi N, Gutteridge JMC. Antioxidant binding of caeruloplasmin to myeloperoxidase: myeloperoxidase is inhibited, but oxidase, peroxidase and immunoreactive properties of caeruloplasmin remain intact. Free Radic Res 2000; 33: 261-265.
208. Griffin SV, Chapman PT, Lianos EA, Lockwood CM. The inhibition of myeloperoxidase by ceruloplasmin can be reversed by anti-myeloperoxidase antibodies. Kidney Int 1999; 55: 917-925.
209. Sokolov AV, Ageeva KV, Cherkalina OS, and et al. Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin. Chem Phys Lipids 2010; 163: 347-355.
210. Baldus S, Rudolph V, Roiss M, and et al. Heparins increase endothelial nitric oxide bioavailability by liberating vessel-immobilized myeloperoxidase. Circulation 2006; 113: 1871-1878.
211. Kettle AJ, Winterbourn CC. Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs. Biochem Pharmacol 1991; 41: 1485-1492.
212. Whiteman M, Rose P, Halliwell B. Inhibition of hypochlorous acid-induced oxidative reactions by nitrite: is nitrite an antioxidant? Biochem Biophys Res Commun 2003; 303: 1217-1224.
213. Graham GG, Day RO, Milligan MK, Ziegler JB, Kettle AJ. Current concepts of the actions of paracetamol (acetaminophen) and NSAIDs. Inflammopharmacology 1999; 7: 255-263.
214. Jantschko W, Furtmüller PG, Zederbauer M, and et al. Exploitation of the unusual thermodynamic properties of human myeloperoxidase in inhibitor design. Biochem Pharmacol 2005; 69: 1149-1157. (Pubitemid 40417486)
215. Rees MD, Bottle SE, Fairfull-Smith KE, Malle E, Whitelock JM, Davies MJ. Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides. Biochem J 2009; 421: 79-86.
216. Meotti FC, Senthilmohan R, Harwood DT, Missau FC, Pizzolatti MG, Kettle AJ. Myricitrin as a substrate and inhibitor of myeloperoxidase: implications for the pharmacological effects of flavonoids. Free Radic Biol Med 2008; 44: 109-120. (Pubitemid 350138636)
217. Loke WM, Proudfoot JM, McKinley AJ, and et al. Quercetin and its in vivo metabolites inhibit neutrophil-mediated low-density lipoprotein oxidation. J Agric Food Chem 2008; 56: 3609-3615.
218. Crozier A, Jaganath IB, Clifford MN. Dietary phenolics: chemistry, bioavailability and effects on health. Nat Prod Rep 2009; 26: 1001-1043.
219. Kettle AJ, Candaeis LP. Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production. Redox Rep 2000; 5: 179-184.
220. Galijasevic S, Abdulhamid I, Abu-Soud HM. Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase. Free Radic Biol Med 2008; 44: 1570-1577.
221. Ximenes VF, Paino IM, Faria-Oliveira OM, Fonseca LM, Brunetti IL. Indole ring oxidation by activated leukocytes prevents the production of hypochlorous acid. Braz J Med Biol Res 2005; 38: 1575-1583.
222. Sliskovic I, Abdulhamid I, Sharma M, Abu-Soud HM. Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase. Free Radic Biol Med 2009; 47: 1005-1013.
223. Mitchell JB, Xavier S, DeLuca AM, and et al. A low molecular weight antioxidant decreases weight and lowers tumour incidence. Free Radic Biol Med 2003; 34: 93-102. (Pubitemid 36043890)
224. Burner U, Obinger C, Paumann M, Furtmüler PG, Kettle AJ. Transient and steady-state kinetics of the oxidation of substituted benzoic acid hydrazides by myeloperoxidase. J Biol Chem 1999; 274: 9494-9502. (Pubitemid 129517923)
225. Kettle AJ, Gedye CA, Hampton MB, Winterbourn CC. Inhibition of myeloperoxidase by benzoic acid hydrazides. Biochem J 1995; 308: 559-563.
226. Kettle AJ, Gedye CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide. Biochem J 1997; 321: 503-508.
227. van Zyl, Basson K, Uebel RA, van der Walt BJ. Isoniazid-mediated irreversible inhibition of the myeloperoxidase antimicrobial system of the human neutrophil and the effect of thyronines. Biochem Pharmacol 1989; 38: 2363-2373.