Reactivity of selenium-containing compounds with myeloperoxidase-derived chlorinating oxidants: Second-order rate constants and implications for biological damage

Free Radical Biology and Medicine

Volumn 84, Issue , 2015, Pages 279-288

  Carroll, Luke ^a,b   Pattison, David I ^a,b   Fu, Shanlin ^c   Schiesser, Carl H ^d   Davies, Michael J ^a,b,e   Hawkins, Clare L ^a,b  

^a HEART RESEARCH INSTITUTE   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

^c UNIVERSITY OF TECHNOLOGY SYDNEY   (Australia)

^d UNIVERSITY OF MELBOURNE   (Australia)

^e UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Hypochlorous acid; Inflammation; Myeloperoxidase; N Chloramines; Oxidation; Selenium

Indexed keywords

CHLORAMINE DERIVATIVE; GLUTATHIONE; HYPOCHLOROUS ACID; METHIONINE; METHYL SELENOCYSTEINE; MYELOPEROXIDASE; OXIDIZING AGENT; SELENIUM DERIVATIVE; SELENOCYSTEINE; SULFUR DERIVATIVE; UNCLASSIFIED DRUG; PEROXIDASE; SCAVENGER;

ARTICLE; ATHEROSCLEROSIS; CHRONIC INFLAMMATION; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HOST PATHOGEN INTERACTION; HUMAN; HUMAN CELL; IMMUNE RESPONSE; KINETICS; MASS SPECTROMETRY; NEUTROPHIL; NORMAL HUMAN; OXIDATION; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; CHEMISTRY;

CHLORAMINES; FREE RADICAL SCAVENGERS; KINETICS; OXIDANTS; PEROXIDASE; SELENIUM COMPOUNDS;

EID: 84929091787     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.03.029     Document Type: Article

References (57)

1. M.J. Davies, C.L. Hawkins, D.I. Pattison, and M.D. Rees Mammalian heme peroxidases: from molecular mechanisms to health implications Antioxid. Redox Signal. 10 2008 1199 1234
2. S.J. Klebanoff Myeloperoxidase: friend and foe J. Leukocyte Biol. 77 2005 598 625
3. C.J. Van Dalen, M.W. Whitehouse, C.C. Winterbourn, and A.J. Kettle Thiocyanate and chloride as competing substrates for myeloperoxidase Biochem. J. 327 1997 487 492
4. P.E. Morgan, D.I. Pattison, J. Talib, F.A. Summers, J.A. Harmer, D.S. Celermajer, C.L. Hawkins, and M.J. Davies High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase Free Radic. Biol. Med. 51 2011 1815 1822
5. M.B. Hampton, A.J. Kettle, and C.C. Winterbourn Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing Blood 92 1998 3007 3017
6. D.I. Pattison, and M.J. Davies Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases Curr. Med. Chem. 13 2006 3271 3290
7. C. Storkey, M.J. Davies, and D.I. Pattison Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach Free Radic. Biol. Med. 73 2014 60 66
8. B.S. Rayner, D.T. Love, and C.L. Hawkins Comparative reactivity of myeloperoxidase-derived oxidants with mammalian cells Free Radic. Biol. Med. 71 2014 240 255
9. E.L. Thomas, M.B. Grisham, and M.M. Jefferson Preparation and characterization of chloramines Methods Enzymol. 132 1986 569 585
10. C.L. Hawkins, and M.J. Davies Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation, reactions of nitrogen-centred radicals J. Chem. Soc. Perkin Trans 2 1998 1937 1945
11. X.L. Armesto, M. Canle, M.V. Garcia, and J.A. Santaballa Aqueous chemistry of N-halo-compounds Chem. Soc. Rev. 27 1998 453 460
12. G.B. Schuller-Levis, and E. Park Taurine: new implications for an old amino acid FEMS Microbiol. Lett. 226 2003 195 202
13. C.L. Hawkins, D.I. Pattison, and M.J. Davies Hypochlorite-induced oxidation of amino acids, peptides and proteins Amino Acids 25 2003 259 274
14. A.V. Peskin, and C.C. Winterbourn Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate Free Radic. Biol. Med. 30 2001 572 579
15. A.V. Peskin, and C.C. Winterbourn Histamine chloramine reactivity with thiol compounds, ascorbate, and methionine and with intracellular glutathione Free Radic. Biol. Med. 35 2003 1252 1260
16. A.V. Peskin, and C.C. Winterbourn 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. 40 2006 45 53
17. A.V. Peskin, R.G. Midwinter, D.T. Harwood, and C.C. Winterbourn Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity Free Radic. Biol. Med. 37 2004 1622 1630
18. M.C.M. Vissers, W.G. Lee, and M.B. Hampton Regulation of apoptosis by vitamin C - specific protection of the apoptotic machinery against exposure to chlorinated oxidants J. Biol. Chem. 276 2001 46835 46840
19. A.C. Carr, C.L. Hawkins, S.R. Thomas, R. Stocker, and B. Frei Relative reactivities of N-chloramines and hypochlorous acid with human plasma constituents Free Radic. Biol. Med. 30 2001 526 536
20. D.I. Pattison, C.L. Hawkins, and M.J. Davies What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach Chem. Res. Toxicol. 22 2009 807 817
21. C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
22. C. Storkey, M.J. Davies, J.M. White, and C.H. Schiesser Synthesis and antioxidant capacity of 5-selenopyranose derivatives Chem. Commun. 47 2011 9693 9695
23. O. Skaff, D.I. Pattison, P.E. Morgan, R. Bachana, V.K. Jain, K.I. Priyadarsini, and M.J. Davies Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage Biochem. J. 441 2012 305 316
24. P. Nagy, G.N.L. Jameson, and C.C. Winterbourn Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione Chem. Res. Toxicol. 22 2009 1833 1840
25. R.E. Huber, and R.S. Criddle Comparison of chemical properties of selenocysteine and selenocystine with their sulfur analogs Arch. Biochem. Biophys. 122 1967 164 173
26. S. Padmaja, G.L. Squadrito, J.N. Lemercier, R. Cueto, and W.A. Pryor Rapid oxidation of DL-selenomethionine by peroxynitrite Free Radic. Biol. Med. 21 1996 317 322
27. C. Storkey, D.I. Pattison, J.M. White, C.H. Schiesser, and M.J. Davies Preventing protein oxidation with sugars: scavenging of hypohalous acids by 5-selenopyranose and 4-selenofuranose derivatives Chem. Res. Toxicol. 25 2012 2589 2599
28. A. Assmann, K. Briviba, and H. Sies Reduction of methionine selenoxide to selenomethionine by glutathione Arch. Biochem. Biophys. 349 1998 201 203
29. R.J. Krause, and A.A. Elfarra Reduction of L-methionine selenoxide to seleno-L-methionine by endogenous thiols, ascorbic acid, or methimazole Biochem. Pharmacol. 77 2009 134 140
30. F. Kumakura, B. Mishra, K.I. Priyadarsini, and M. Iwaoka A water-soluble cyclic selenide with enhanced glutathione peroxidase-like catalytic activities Eur. J. Org. Chem. 2010 2010 440 445
31. E.L. Thomas, M.B. Grisham, and M.M. Jefferson Cytotoxicity of chloramines Methods Enzymol. 132 1986 585 593
32. F.A. Summers, P.E. Morgan, M.J. Davies, and C.L. Hawkins Identification of plasma proteins that are susceptible to thiol oxidation by hypochlorous acid and N-chloramines Chem. Res. Toxicol. 21 2008 1832 1840
33. C.L. Hawkins, P.E. Morgan, and M.J. Davies Quantification of protein modification by oxidants Free Radic. Biol. Med. 46 2009 965 988
34. P. Eyer, F. Worek, D. Kiderlen, G. Sinko, A. Stuglin, V. Simeon-Rudolf, and E. Reiner Molar absorption coefficients for the reduced Ellman reagent: reassessment Anal. Biochem. 312 2003 224 227
35. J.M. Dypbukt, C. Bishop, W.M. Brooks, B. Thong, H. Eriksson, and A.J. Kettle A sensitive and selective assay for chloramine production by myeloperoxidase Free Radic. Biol. Med. 39 2005 1468 1477
36. A. Ferrante, and Y.H. Thong Optimal conditions for simultaneous purification of mononuclear and polymorphonuclear leucocytes from human blood by the hypaque-ficoll method J. Immunol. Methods 36 1980 109 117
37. D.I. Pattison, and M.J. Davies Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation Biochemistry 44 2005 7378 7387
38. D.I. Pattison, and M.J. Davies Evidence for rapid inter- and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous-acid-mediated damage Biochemistry 45 2006 8152 8162
39. R.J. Krause, S.C. Glocke, A.R. Sicuri, S.L. Ripp, and A.A. Elfarra Oxidative metabolism of seleno-L-methionine to L-methionine selenoxide by flavin-containing monooxygenases Chem. Res. Toxicol. 19 2006 1643 1649
40. A.V. Peskin, R. Turner, G.J. Maghzal, C.C. Winterbourn, and A.J. Kettle Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils Biochemistry 48 2009 10175 10182
41. J.L. Beal, S.B. Foster, and M.T. Ashby Hypochlorous acid reacts with the N-terminal methionines of proteins to give dehydromethionine, a potential biomarker for neutrophil-induced oxidative stress Biochemistry 48 2009 11142 11148
42. F.A. Summers, A.F. Quigley, and C.L. Hawkins Identification of proteins susceptible to thiol oxidation in endothelial cells exposed to hypochlorous acid and N-chloramines Biochem. Biophys Res. Commun. 425 2012 157 161
43. A.S. Rahmanto, and M.J. Davies Catalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides Free Radic. Biol. Med. 51 2011 2288 2299
44. H. Sies, L. Klotz, V. Sharov, A. Assmann, and K. Briviba Protection against peroxynitrite by selenoproteins Z. Naturforsch. C 53 1998 228 232
45. H. Steinbrenner, and H. Sies Protection against reactive oxygen species by selenoproteins Biochem. Biophys. Acta 1790 2009 1478 1485
46. B. Gammelgaard, C. Cornett, J. Olsen, L. Bendahl, and S.H. Hansen Combination of LC-ICP-MS, LC-MS and NMR for investigation of the oxidative degradation of selenomethionine Talanta 59 2003 1165 1171
47. D.I. Pattison, C.L. Hawkins, and M.J. Davies Hypochlorous acid-mediated protein oxidation: how important are chloramine transfer reactions and protein tertiary structure? Biochemistry 46 2007 9853 9864
48. J.W. Heinecke Pathways for oxidation of low density lipoprotein by myeloperoxidase: tyrosyl radical, reactive aldehydes, hypochlorous acid and molecular chlorine BioFactors 6 1997 145 155
49. M. Iwaoka, T. Takahashi, and S. Tomoda Syntheses and structural characterization of water-soluble selenium reagents for the redox control of protein disulfide bonds Heteroatom Chem. 12 2001 293 299
50. M. Iwaoka, and S. Tomoda Trans-3,4-dihydroxy-1-selenolane oxide: a new reagent for rapid and quantitative formation of disulfide bonds in polypeptides Chem. Lett. 2000 1400 1401
51. A. Müller, E. Cadenas, P. Graf, and H. Sies A novel biologically active seleno-organic compound-1: glutathione peroxidase-like activity in vitro and antioxidant capacity of pz 51 (Ebselen) Biochem. Pharmacol. 33 1984 3235 3239
52. H. Fischer, and N. Dereu Mechanism of the catalytic reduction of hydroperoxides by ebselen: a selenium 77 NMR study Bull. Soc. Chim. Belges 96 1987 757 768
53. S. Miller, S.W. Walker, J.R. Arthur, F. Nicol, K. Pickard, M.H. Lewin, A.F. Howie, and G.J. Beckett Selenite protects human endothelial cells from oxidative damage and induces thioredoxin reductase Clin. Sci. 100 2001 543 550
54. A. Khera, J.J. Vanderlelie, and A.V. Perkins Selenium supplementation protects trophoblast cells from mitochondrial oxidative stress Placenta 34 2013 594 598
55. S.L. Hazen, and J.W. Heinecke 3-chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima J. Clin. Invest. 99 1997 2075 2081
56. R. Zhang, M.-L. Brennan, X. Fu, R.J. Aviles, G.L. Pearce, M.S. Penn, E.J. Topol, D.L. Sprecher, and S.L. Hazen Association between myeloperoxidase levels and risk of coronary artery disease J. Am. Med. Assoc. 286 2001 2136 2142
57. M.-L. Brennan, M.S. Penn, F. Van Lente, V. Nambi, M.H. Shishehbor, R. Aviles, M. Goormastic, M.L. Pepoy, E.S. McErlean, E.J. Topol, S.E. Nissen, and S.L. Hazen Prognostic value of myeloperoxidase in patients with chest pain N. Engl. J. Med. 349 2003 1595 1604