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Volumn 422, Issue 1, 2009, Pages 111-117

Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: Absolute rate constants and assessment of biological relevance

Author keywords

Hypothiocyanous acid (HOSCN); Kinetics; Lactoperoxidase; Myeloperoxidase; Thiols

Indexed keywords

ACETYL-CYSTEINE; CREATINE KINASE; CYSTEINE RESIDUES; EOSINOPHIL PEROXIDASE; HYPOBROMOUS ACID; HYPOCHLOROUS ACIDS; HYPOTHIOCYANOUS ACID (HOSCN); INVERSE RELATIONSHIP; KINETIC DATA; LACTOGLOBULIN; LACTOPEROXIDASE; MYELOPEROXIDASE; NITROBENZOIC ACIDS; OXIDATIVE DAMAGE; OXIDIZING AGENTS; PHYSIOLOGICAL CONCENTRATIONS; PROTEIN THIOLS; RATE OF REACTION; SECOND-ORDER RATE CONSTANTS; THIOL GROUPS; THIOL OXIDATION; THIOLS;

EID: 68749097272     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090276     Document Type: Article
Times cited : (114)

References (48)
  • 1
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies, M. J., Hawkins, C. L., Pattison, D. I. and Rees, M. D. (2008) Mammalian heme peroxidases: From molecular mechanisms to health implications. Antioxid. Redox Signaling 10, 1199-1234
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 2
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle, A. J. and Winterbourn, C. C. (1997) Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep. 3, 3-15
    • (1997) Redox Rep , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 3
    • 0034254665 scopus 로고    scopus 로고
    • On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids
    • Prutz, W. A., Kissner, R., Koppenol, W. H. and Ruegger, H. (2000) On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids. Arch. Biochem. Biophys. 380, 181-191
    • (2000) Arch. Biochem. Biophys , vol.380 , pp. 181-191
    • Prutz, W.A.1    Kissner, R.2    Koppenol, W.H.3    Ruegger, H.4
  • 4
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5?C to 35?C
    • Morris, J. C. (1966) The acid ionization constant of HOCl from 5?C to 35?C. J. Phys. Chem. 70, 3798-3805
    • (1966) J. Phys. Chem , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 5
    • 0019889026 scopus 로고
    • Lactoperoxidase-catalyzed oxidation of thiocyanate: Equilibriums between oxidized forms of thiocyanate
    • Thomas, E. L. (1981) Lactoperoxidase-catalyzed oxidation of thiocyanate: equilibriums between oxidized forms of thiocyanate. Biochemistry 20, 3273-3280
    • (1981) Biochemistry , vol.20 , pp. 3273-3280
    • Thomas, E.L.1
  • 7
    • 0030660227 scopus 로고    scopus 로고
    • Thiocyanate and chloride as competing substrates for myeloperoxidase
    • Van Dalen, C. J., Whitehouse, M. W., Winterbourn, C. C. and Kettle, A. J. (1997) Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J. 327, 487-492
    • (1997) Biochem J , vol.327 , pp. 487-492
    • Van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 8
    • 0028815793 scopus 로고
    • Thiocyanate, a plausible physiological electron-donor of gastric peroxidase
    • Das, D., De, P. K. and Banerjee, R. K. (1995) Thiocyanate, a plausible physiological electron-donor of gastric peroxidase. Biochem. J. 305, 59-64
    • (1995) Biochem. J , vol.305 , pp. 59-64
    • Das, D.1    De, P.K.2    Banerjee, R.K.3
  • 9
    • 30544441504 scopus 로고    scopus 로고
    • Origin, structure, and biological activities of peroxidases in human saliva
    • Ihalin, R., Loimaranta, V. and Tenovuo, J. (2006) Origin, structure, and biological activities of peroxidases in human saliva. Arch. Biochem. Biophys. 445, 261-268
    • (2006) Arch. Biochem. Biophys , vol.445 , pp. 261-268
    • Ihalin, R.1    Loimaranta, V.2    Tenovuo, J.3
  • 11
    • 10344256217 scopus 로고    scopus 로고
    • Redox buffering of hypochlorous acid by thiocyanate in physiologic fluids
    • Ashby, M. T., Carlson, A. C. and Scott, M. J. (2004) Redox buffering of hypochlorous acid by thiocyanate in physiologic fluids. J. Am. Chem. Soc. 126, 15976-15977
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15976-15977
    • Ashby, M.T.1    Carlson, A.C.2    Scott, M.J.3
  • 12
    • 33646078598 scopus 로고    scopus 로고
    • Thiocyanate is an efficient endogenous scavenger of the phagocytic killing agent hypobromous acid
    • Nagy, P., Beal, J. L. and Ashby, M. T. (2006) Thiocyanate is an efficient endogenous scavenger of the phagocytic killing agent hypobromous acid. Chem. Res. Toxicol. 19, 587-593
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 587-593
    • Nagy, P.1    Beal, J.L.2    Ashby, M.T.3
  • 13
    • 0018386333 scopus 로고
    • Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: Nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli
    • Thomas, E. L. (1979) Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli. Infect. Immun. 23, 522-531
    • (1979) Infect. Immun , vol.23 , pp. 522-531
    • Thomas, E.L.1
  • 14
    • 0034457129 scopus 로고    scopus 로고
    • Living with a killer: The effects of hypochlorous acid on mammalian cells
    • Pullar, J. M., Vissers, M. C. and Winterbourn, C. C. (2000) Living with a killer: the effects of hypochlorous acid on mammalian cells. IUBMB Life 50, 259-266
    • (2000) IUBMB Life , vol.50 , pp. 259-266
    • Pullar, J.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 15
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • Pattison, D. I. and Davies, M. J. (2006) Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases. Curr. Med. Chem. 13, 3271-3290
    • (2006) Curr. Med. Chem , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 16
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds
    • Pattison, D. I. and Davies, M. J. (2001) Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds. Chem. Res. Toxicol. 14, 1453-1464
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 17
    • 0003698541 scopus 로고
    • Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leukocyte myeloperoxidase
    • Albrich, J. M., McCarthy, C. A. and Hurst, J. K. (1981) Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase. Proc. Natl. Acad. Sci. U.S.A. 78, 210-214
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 210-214
    • Albrich, J.M.1    McCarthy, C.A.2    Hurst, J.K.3
  • 18
    • 0020491334 scopus 로고
    • Oxidation of Escherichia coli iron centers by the myeloperoxidase-mediated microbicidal system
    • Rosen, H. and Klebanoff, S. (1982) Oxidation of Escherichia coli iron centers by the myeloperoxidase-mediated microbicidal system. J. Biol. Chem. 257, 13731-13735
    • (1982) J. Biol. Chem , vol.257 , pp. 13731-13735
    • Rosen, H.1    Klebanoff, S.2
  • 20
    • 0344393610 scopus 로고    scopus 로고
    • Fragmentation of extracellular matrix by hypochlorous acid
    • Woods, A. A. and Davies, M. J. (2003) Fragmentation of extracellular matrix by hypochlorous acid. Biochem. J. 376, 219-227
    • (2003) Biochem. J , vol.376 , pp. 219-227
    • Woods, A.A.1    Davies, M.J.2
  • 21
    • 0035808392 scopus 로고    scopus 로고
    • Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system
    • Arlandson, M., Decker, T., Roongta, V. A., Bonilla, L., Mayo, K. H., MacPherson, J. C., Hazen, S. L. and Slungaard, A. (2001) Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J. Biol. Chem. 276, 215-224
    • (2001) J. Biol. Chem , vol.276 , pp. 215-224
    • Arlandson, M.1    Decker, T.2    Roongta, V.A.3    Bonilla, L.4    Mayo, K.H.5    MacPherson, J.C.6    Hazen, S.L.7    Slungaard, A.8
  • 22
    • 58949087905 scopus 로고    scopus 로고
    • Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation
    • Hawkins, C. L., Pattison, D. I., Stanley, N. R. and Davies, M. J. (2008) Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation. Biochem. J. 416, 441-452
    • (2008) Biochem. J , vol.416 , pp. 441-452
    • Hawkins, C.L.1    Pattison, D.I.2    Stanley, N.R.3    Davies, M.J.4
  • 23
    • 50949098899 scopus 로고    scopus 로고
    • Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid
    • Lloyd, M. M., Van Reyk, D. M., Davies, M. J. and Hawkins, C. L. (2008) 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. 414, 271-280
    • (2008) Biochem J , vol.414 , pp. 271-280
    • Lloyd, M.M.1    Van Reyk, D.M.2    Davies, M.J.3    Hawkins, C.L.4
  • 24
    • 0030565016 scopus 로고    scopus 로고
    • A comparison of the quantitation of macrophage foam cell populations and the extent of apolipoprotein E deposition in developing atherosclerotic lesions in young people: High and low serum thiocyanate groups as an indication of smoking
    • Botti, T. P., Amin, H., Hiltscher, L. and Wissler, R. W. (1996) A comparison of the quantitation of macrophage foam cell populations and the extent of apolipoprotein E deposition in developing atherosclerotic lesions in young people: high and low serum thiocyanate groups as an indication of smoking. Atherosclerosis. 124, 191-202
    • (1996) Atherosclerosis , vol.124 , pp. 191-202
    • Botti, T.P.1    Amin, H.2    Hiltscher, L.3    Wissler, R.W.4
  • 25
    • 0342902619 scopus 로고    scopus 로고
    • Evidence for more extensive deposits of epitopes of oxidized low density lipoproteins in aortas of young people with elevated serum thiocyanate levels
    • Scanlon, C. E. O., Berger, B., Malcom, G. and Wissler, R. W. (1996) Evidence for more extensive deposits of epitopes of oxidized low density lipoproteins in aortas of young people with elevated serum thiocyanate levels. Atherosclerosis 121, 23-33
    • (1996) Atherosclerosis , vol.121 , pp. 23-33
    • Scanlon, C.E.O.1    Berger, B.2    Malcom, G.3    Wissler, R.W.4
  • 29
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • Hawkins, C. L. and Davies, M. J. (1998) Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem. J. 332, 617-625
    • (1998) Biochem. J , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 30
    • 38149073446 scopus 로고    scopus 로고
    • Kinetics of hypobromous acid-mediated oxidation of lipid components and antioxidants
    • Skaff, O., Pattison, D. I. and Davies, M. J. (2007) Kinetics of hypobromous acid-mediated oxidation of lipid components and antioxidants. Chem. Res. Toxicol. 20, 1980-1988
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 1980-1988
    • Skaff, O.1    Pattison, D.I.2    Davies, M.J.3
  • 31
    • 48649109320 scopus 로고    scopus 로고
    • The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: A kinetic study
    • Skaff, O., Pattison, D. I. and Davies, M. J. (2008) The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study. Biochemistry 47, 8237-8245
    • (2008) Biochemistry , vol.47 , pp. 8237-8245
    • Skaff, O.1    Pattison, D.I.2    Davies, M.J.3
  • 33
    • 0037155215 scopus 로고    scopus 로고
    • Determinants of the phagosomal pH in neutrophils
    • Jankowski, A., Scott, C. C. and Grinstein, S. (2002) Determinants of the phagosomal pH in neutrophils. J. Biol. Chem. 277, 6059-6066
    • (2002) J. Biol. Chem , vol.277 , pp. 6059-6066
    • Jankowski, A.1    Scott, C.C.2    Grinstein, S.3
  • 34
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. (1988) Glutathione metabolism and its selective modification. J. Biol. Chem. 263, 17205-17208
    • (1988) J. Biol. Chem , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 35
    • 0030708939 scopus 로고    scopus 로고
    • Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
    • Carr, A. C. and Winterbourn, C. C. (1997) Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem. J. 327, 275-281
    • (1997) Biochem. J , vol.327 , pp. 275-281
    • Carr, A.C.1    Winterbourn, C.C.2
  • 36
    • 0035933821 scopus 로고    scopus 로고
    • Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide
    • Pullar, J. M., Vissers, M. C. and Winterbourn, C. C. (2001) Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide. J. Biol. Chem. 276, 22120-22125
    • (2001) J. Biol. Chem , vol.276 , pp. 22120-22125
    • Pullar, J.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 37
    • 0001582001 scopus 로고
    • Reactions of the cyanate present in aqueous urea with amino acids and proteins
    • Stark, G. R., Stein, W. H. and Moore, S. (1960) Reactions of the cyanate present in aqueous urea with amino acids and proteins. J. Biol. Chem. 235, 3177-3181
    • (1960) J. Biol. Chem , vol.235 , pp. 3177-3181
    • Stark, G.R.1    Stein, W.H.2    Moore, S.3
  • 38
    • 0035283131 scopus 로고    scopus 로고
    • Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate
    • Peskin, A. V. and Winterbourn, C. C. (2001) Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radioal Biol. Med. 30, 572-579
    • (2001) Free Radioal Biol. Med , vol.30 , pp. 572-579
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 39
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase
    • Wang, P. F., McLeish, M. J., Kneen, M. M., Lee, G. and Kenyon, G. L. (2001) An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry 40, 11698-11705
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 40
    • 0031000775 scopus 로고    scopus 로고
    • pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan, U., Mieyal, P. A. and Mieyal, J. J. (1997) pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36, 3199-3206
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 41
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827-835
    • (1998) Nat. Struct. Biol , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 42
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao, J. K., Bujacz, G. and Wlodawer, A. (1998) Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 439, 133-137
    • (1998) FEBS Lett , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3
  • 43
    • 1942502782 scopus 로고    scopus 로고
    • A 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
    • Pattison, D. I. and Davies, M. J. (2004) A 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 43, 4799-4809
    • (2004) Biochemistry , vol.43 , pp. 4799-4809
    • Pattison, D.I.1    Davies, M.J.2
  • 44
    • 0034681349 scopus 로고    scopus 로고
    • First steps in the oxidation of sulfur-containing amino acids by hypohalogenation: Very fast generation of intermediate sulfenyl halides and halosulfonium cations
    • Armesto, X. L., Canle, M., Fernandez, M. I., Garcia, M. V. and Santaballa, J. A. (2000) First steps in the oxidation of sulfur-containing amino acids by hypohalogenation: very fast generation of intermediate sulfenyl halides and halosulfonium cations. Tetrahedron 56, 1103-1109
    • (2000) Tetrahedron , vol.56 , pp. 1103-1109
    • Armesto, X.L.1    Canle, M.2    Fernandez, M.I.3    Garcia, M.V.4    Santaballa, J.A.5
  • 45
    • 67649986506 scopus 로고    scopus 로고
    • What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach
    • Pattison, D. I., Hawkins, C. L. and Davies, M. J. (2009) What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chem. Res. Toxicol. 22, 807-817
    • (2009) Chem. Res. Toxicol , vol.22 , pp. 807-817
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 46
    • 58149214250 scopus 로고    scopus 로고
    • Inorganic chemistry of defensive peroxidases in the human oral cavity
    • Ashby, M. T. (2008) Inorganic chemistry of defensive peroxidases in the human oral cavity. J. Dent. Res. 87, 900-914
    • (2008) J. Dent. Res , vol.87 , pp. 900-914
    • Ashby, M.T.1
  • 47
    • 33846211109 scopus 로고    scopus 로고
    • The lactoperoxidase system links anion transport to host defense in cystic fibrosis
    • Conner, G. E., Wijkstrom-Frei, C., Randell, S. H., Fernandez, V. E. and Salathe, M. (2007) The lactoperoxidase system links anion transport to host defense in cystic fibrosis. FEBS Lett. 581, 271-278
    • (2007) FEBS Lett , vol.581 , pp. 271-278
    • Conner, G.E.1    Wijkstrom-Frei, C.2    Randell, S.H.3    Fernandez, V.E.4    Salathe, M.5


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