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Volumn 51, Issue 2, 2011, Pages 374-386

Reaction of hemoglobin with HOCl: Mechanism of heme destruction and free iron release

Author keywords

Free iron; Free radicals; Hemoglobin; Hypochlorous acid; Inflammation; Mammalian peroxidase; Oxidative stress; RBC

Indexed keywords

CARBON; HEME; HEMOGLOBIN; HYPOCHLOROUS ACID; IRON; PORPHYRIN; TETRAPYRROLE DERIVATIVE;

EID: 79959340510     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.04.011     Document Type: Article
Times cited : (67)

References (75)
  • 3
    • 58149165358 scopus 로고    scopus 로고
    • Hemoglobin research and the origins of molecular medicine
    • A.N. Schechter Hemoglobin research and the origins of molecular medicine Blood 112 2008 3927 3938
    • (2008) Blood , vol.112 , pp. 3927-3938
    • Schechter, A.N.1
  • 4
    • 0019778079 scopus 로고
    • Equality of the in vivo and in vitro oxygen-binding capacity of haemoglobin in patients with severe respiratory disease
    • E.D. Dominguez de Villota, M.T. Ruiz Carmona, J.J. Rubio, and S. de Andres Equality of the in vivo and in vitro oxygen-binding capacity of haemoglobin in patients with severe respiratory disease Br. J. Anaesth. 53 1981 1325 1328 (Pubitemid 12248935)
    • (1981) British Journal of Anaesthesia , vol.53 , Issue.12 , pp. 1325-1328
    • Dominguez De Villota, E.1    Garcia Carmona, M.T.2    Rubio, J.J.3    Ruiz De Andres, S.4
  • 5
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • DOI 10.1089/ars.2004.6.967
    • E. Nagababu, and J.M. Rifkind Heme degradation by reactive oxygen species Antioxid. Redox Signal. 6 2004 967 978 (Pubitemid 39434933)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 6
    • 0035001778 scopus 로고    scopus 로고
    • Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications
    • A.I. Alayash, R.P. Patel, and R.E. Cashon Redox reactions of hemoglobin and myoglobin: biological and toxicological implications Antioxid. Redox Signal. 3 2001 313 327 (Pubitemid 32473345)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.2 , pp. 313-327
    • Alayash, A.I.1    Patel, R.P.2    Cashon, R.E.3
  • 7
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • DOI 10.1016/0076-6879(90)86118-F
    • C.C. Winterbourn Oxidative reactions of hemoglobin Methods Enzymol. 186 1990 265 272 (Pubitemid 20279966)
    • (1990) Methods in Enzymology , vol.186 , pp. 265-272
    • Winterbourn, C.C.1
  • 9
    • 0026948804 scopus 로고
    • Interaction of hypochlorite with oxyhemoglobin leads to liberation of iron in a catalytically active form
    • E. Iakutova, A.N. Osipov, O.V. Kostenko, I. Arnkhol'd, K. Arnol'd, and A. Vladimirov Iu Interaction of hypochlorite with oxyhemoglobin leads to liberation of iron in a catalytically active form Biofizika 37 1992 1021 1028
    • (1992) Biofizika , vol.37 , pp. 1021-1028
    • Iakutova, E.1    Osipov, A.N.2    Kostenko, O.V.3    Arnkhol'D, I.4    Arnol'D, K.5    Vladimirov Iu, A.6
  • 10
    • 0021833801 scopus 로고
    • Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P-450 heme
    • DOI 10.1021/bi00334a027
    • W.H. Schaefer, T.M. Harris, and F.P. Guengerich Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P-450 heme Biochemistry 24 1985 3254 3263 (Pubitemid 15028728)
    • (1985) Biochemistry , vol.24 , Issue.13 , pp. 3254-3263
    • Schaefer, W.H.1    Harris, T.M.2    Guengerich, F.P.3
  • 11
    • 0032534908 scopus 로고    scopus 로고
    • Identification of the heme-modified peptides from cumene hydroperoxide-inactivated cytochrome P450 3A4
    • DOI 10.1021/bi9808464
    • K. He, L.M. Bornheim, A.M. Falick, D. Maltby, H. Yin, and M.A. Correia Identification of the heme-modified peptides from cumene hydroperoxide- inactivated cytochrome P450 3A4 Biochemistry 37 1998 17448 17457 (Pubitemid 29013746)
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17448-17457
    • He, K.1
  • 12
  • 13
    • 0141905917 scopus 로고    scopus 로고
    • Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
    • DOI 10.1042/BJ20030685
    • A.L. Chapman, C.C. Winterbourn, S.O. Brennan, T.W. Jordan, and A.J. Kettle Characterization of non-covalent oligomers of proteins treated with hypochlorous acid Biochem. J. 375 2003 33 40 (Pubitemid 37255379)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 33-40
    • Chapman, A.L.P.1    Winterbourn, C.C.2    Brennan, S.O.3    Jordan, T.W.4    Kettle, A.J.5
  • 15
    • 0032519779 scopus 로고    scopus 로고
    • Comparison of human red cell lysis by hypochlorous and hypobromous acids: Insights into the mechanism of lysis
    • M.C. Vissers, A.C. Carr, and A.L. Chapman Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis Biochem. J. 330 Pt 1 1998 131 138 (Pubitemid 28075731)
    • (1998) Biochemical Journal , vol.330 , Issue.1 , pp. 131-138
    • Vissers, M.C.M.1    Carr, A.C.2    Chapman, A.L.P.3
  • 16
    • 0025980710 scopus 로고
    • Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl
    • M.C. Vissers, and C.C. Winterbourn Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl Arch. Biochem. Biophys. 285 1991 53 59
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 53-59
    • Vissers, M.C.1    Winterbourn, C.C.2
  • 17
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • DOI 10.1016/j.toxlet.2005.03.004, PII S0378427405000883
    • S. Kumar, and U. Bandyopadhyay Free heme toxicity and its detoxification systems in human Toxicol. Lett. 157 2005 175 188 (Pubitemid 40726102)
    • (2005) Toxicology Letters , vol.157 , Issue.3 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 18
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogen-peroxide-induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase
    • DOI 10.1016/S0304-4165(02)00537-8
    • E. Nagababu, F.J. Chrest, and J.M. Rifkind Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase Biochim. Biophys. Acta 1620 2003 211 217 (Pubitemid 36197913)
    • (2003) Biochimica et Biophysica Acta - General Subjects , vol.1620 , Issue.1-3 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 19
    • 51749092207 scopus 로고    scopus 로고
    • Oxidative stress and "senescent" fibroblasts in non-healing wounds as potential therapeutic targets
    • R.A. Clark Oxidative stress and "senescent" fibroblasts in non-healing wounds as potential therapeutic targets J. Invest. Dermatol. 128 2008 2361 2364
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 2361-2364
    • Clark, R.A.1
  • 20
    • 0037173578 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
    • DOI 10.1016/S0162-0134(02)00461-0, PII S0162013402004610
    • R.R. Crichton, S. Wilmet, R. Legssyer, and R.J. Ward Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells J. Inorg. Biochem. 91 2002 9 18 (Pubitemid 34727756)
    • (2002) Journal of Inorganic Biochemistry , vol.91 , Issue.1 , pp. 9-18
    • Crichton, R.R.1    Wilmet, S.2    Legssyer, R.3    Ward, R.J.4
  • 21
    • 1842608817 scopus 로고    scopus 로고
    • Iron, atherosclerosis, and neurodegeneration: A key role for cholesterol in promoting iron-dependent oxidative damage?
    • DOI 10.1196/annals.1306.005
    • W.-Y. Ong, and B. Halliwell Iron, atherosclerosis, and neurodegeneration: a key role for cholesterol in promoting iron-dependent oxidative damage? Ann. N. Y. Acad. Sci. 1012 2004 51 64 (Pubitemid 38453515)
    • (2004) Annals of the New York Academy of Sciences , vol.1012 , pp. 51-64
    • Ong, W.-Y.1    Halliwell, B.2
  • 22
    • 0036077111 scopus 로고    scopus 로고
    • Molecular pathogenesis of iron overload
    • DOI 10.1136/gut.51.2.290
    • D. Trinder, C. Fox, G. Vautier, and J.K. Olynyk Molecular pathogenesis of iron overload Gut 51 2002 290 295 (Pubitemid 34791465)
    • (2002) Gut , vol.51 , Issue.2 , pp. 290-295
    • Trinder, D.1    Fox, C.2    Vautier, G.3    Olynyk, J.K.4
  • 24
    • 0034457129 scopus 로고    scopus 로고
    • Living with a killer: The effects of hypochlorous acid on mammalian cells
    • DOI 10.1080/15216540051080958
    • J.M. Pullar, M.C.M. Vissers, and C.C. Winterbourn Living with a killer: the effects of hypochlorous acid on mammalian cells IUBMB Life 50 2000 259 266 (Pubitemid 32289083)
    • (2000) IUBMB Life , vol.50 , Issue.4-5 , pp. 259-266
    • Pullar, J.M.1    Vissers, M.C.M.2    Winterbourn, C.C.3
  • 27
    • 0141727730 scopus 로고    scopus 로고
    • Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes
    • DOI 10.1161/01.CIR.0000090690.67322.51
    • S. Baldus, C. Heeschen, T. Meinertz, A.M. Zeiher, J.P. Eiserich, T. Munzel, M.L. Simoons, and C.W. Hamm Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes Circulation 108 2003 1440 1445 (Pubitemid 37176448)
    • (2003) Circulation , vol.108 , Issue.12 , pp. 1440-1445
    • Baldus, S.1    Heeschen, C.2    Meinertz, T.3    Zeiher, A.M.4    Eiserich, J.P.5    Munzel, T.6    Simoons, M.L.7    Hamm, C.W.8
  • 28
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • DOI 10.1016/S0076-6879(94)33056-5
    • A.J. Kettle, and C.C. Winterbourn Assays for the chlorination activity of myeloperoxidase Methods Enzymol. 233 1994 502 512 (Pubitemid 24177576)
    • (1994) Methods in Enzymology , vol.233 , pp. 502-512
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 29
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • S.J. Weiss, R. Klein, A. Slivka, and M. Wei Chlorination of taurine by human neutrophils: evidence for hypochlorous acid generation J. Clin. Invest. 70 1982 598 607 (Pubitemid 12054584)
    • (1982) Journal of Clinical Investigation , vol.70 , Issue.3 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 30
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • S.J. Weiss Tissue destruction by neutrophils N. Engl. J. Med. 320 1989 365 376 (Pubitemid 19106873)
    • (1989) New England Journal of Medicine , vol.320 , Issue.6 , pp. 365-376
    • Weiss, S.J.1
  • 31
    • 0023269405 scopus 로고
    • Immunology-neutrophils in human diseases
    • H.L. Malech, and J.I. Gallin Immunology-neutrophils in human diseases N. Engl. J. Med. 317 1987 687 694
    • (1987) N. Engl. J. Med. , vol.317 , pp. 687-694
    • Malech, H.L.1    Gallin, J.I.2
  • 32
    • 0344514747 scopus 로고    scopus 로고
    • Myeloperoxidase in kidney disease
    • DOI 10.1046/j.1523-1755.2003.00336.x
    • E. Malle, T. Buch, and H.J. Grone Myeloperoxidase in kidney disease Kidney Int. 64 2003 1956 1967 (Pubitemid 37449530)
    • (2003) Kidney International , vol.64 , Issue.6 , pp. 1956-1967
    • Malle, E.1    Buch, T.2    Grone, H.-J.3
  • 33
    • 0042062310 scopus 로고    scopus 로고
    • Chemical basis of inflammation-induced carcinogenesis
    • DOI 10.1016/S0003-9861(03)00283-2
    • H. Ohshima, M. Tatemichi, and T. Sawa Chemical basis of inflammation-induced carcinogenesis Arch. Biochem. Biophys. 417 2003 3 11 (Pubitemid 36960042)
    • (2003) Archives of Biochemistry and Biophysics , vol.417 , Issue.1 , pp. 3-11
    • Ohshima, H.1    Tatemichi, M.2    Sawa, T.3
  • 34
    • 0141761418 scopus 로고    scopus 로고
    • Contribution of reactive oxygen species to cartilage degradation in rheumatic diseases: Molecular pathways, diagnosis and potential therapeutic strategies
    • DOI 10.2174/0929867033456828
    • J. Schiller, B. Fuchs, J. Arnhold, and K. Arnold Contribution of reactive oxygen species to cartilage degradation in rheumatic diseases: molecular pathways, diagnosis and potential therapeutic strategies Curr. Med. Chem. 10 2003 2123 2145 (Pubitemid 37139067)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.20 , pp. 2123-2145
    • Schiller, J.1    Fuchs, B.2    Arnhold, J.3    Arnold, K.4
  • 37
    • 40749162395 scopus 로고    scopus 로고
    • Contents of endometriotic cysts, especially the high concentration of free iron, are a possible cause of carcinogenesis in the cysts through the iron-induced persistent oxidative stress
    • DOI 10.1158/1078-0432.CCR-07-1614
    • K. Yamaguchi, M. Mandai, S. Toyokuni, J. Hamanishi, T. Higuchi, K. Takakura, and S. Fujii Contents of endometriotic cysts, especially the high concentration of free iron, are a possible cause of carcinogenesis in the cysts through the iron-induced persistent oxidative stress Clin. Cancer Res. 14 2008 32 40 (Pubitemid 351377975)
    • (2008) Clinical Cancer Research , vol.14 , Issue.1 , pp. 32-40
    • Yamaguchi, K.1    Mandai, M.2    Toyokuni, S.3    Hamanishi, J.4    Higuchi, T.5    Takakura, K.6    Fujii, S.7
  • 38
    • 0015040637 scopus 로고
    • Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine)
    • P. Carter Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine) Anal. Biochem. 40 1971 450 458
    • (1971) Anal. Biochem. , vol.40 , pp. 450-458
    • Carter, P.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • P.E. Thomas, D. Ryan, and W. Levin An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels Anal. Biochem. 75 1976 168 176
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 42
    • 0035874521 scopus 로고    scopus 로고
    • Red blood cells inhibit activation-induced cell death and oxidative stress in human peripheral blood T lymphocytes
    • A.M. Fonseca, G. Porto, K. Uchida, and F.A. Arosa Red blood cells inhibit activation-induced cell death and oxidative stress in human peripheral blood T lymphocytes Blood 97 2001 3152 3160
    • (2001) Blood , vol.97 , pp. 3152-3160
    • Fonseca, A.M.1    Porto, G.2    Uchida, K.3    Arosa, F.A.4
  • 46
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • DOI 10.1006/bbrc.1998.8846
    • E. Nagababu, and J.M. Rifkind Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide Biochem. Biophys. Res. Commun. 247 1998 592 596 (Pubitemid 28418436)
    • (1998) Biochemical and Biophysical Research Communications , vol.247 , Issue.3 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 47
    • 0024269252 scopus 로고
    • Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide
    • S. Harel, M.A. Salan, and J. Kanner Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide Free Radic. Res. Commun. 5 1988 11 19
    • (1988) Free Radic. Res. Commun. , vol.5 , pp. 11-19
    • Harel, S.1    Salan, M.A.2    Kanner, J.3
  • 48
    • 0022020912 scopus 로고
    • The degradation of cytochrome c by hydrogen peroxide
    • T.M. Florence The degradation of cytochrome c by hydrogen peroxide J. Inorg. Biochem. 23 1985 131 141
    • (1985) J. Inorg. Biochem. , vol.23 , pp. 131-141
    • Florence, T.M.1
  • 49
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • H.F. Bunn, and J.H. Jandl Exchange of heme among hemoglobins and between hemoglobin and albumin J. Biol. Chem. 243 1968 465 475
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 52
    • 70349917849 scopus 로고    scopus 로고
    • Isolation of a mRNA preferentially expressed in synoviocytes from rheumatoid arthritis that is identical with lumican, which encodes a collagen binding, extracellular matrix protein
    • H. Mori, K. Nishida, T. Ozaki, H. Inoue, and T. Nakanishi Isolation of a mRNA preferentially expressed in synoviocytes from rheumatoid arthritis that is identical with lumican, which encodes a collagen binding, extracellular matrix protein J. Hard Tissue Biol. 17 2008 125 130
    • (2008) J. Hard Tissue Biol. , vol.17 , pp. 125-130
    • Mori, H.1    Nishida, K.2    Ozaki, T.3    Inoue, H.4    Nakanishi, T.5
  • 53
    • 0020479097 scopus 로고
    • Mechanism of inhibition of horseradish peroxidase by cyclopropanone hydrate
    • J.S. Wiseman, J.S. Nichols, and M.X. Kolpak Mechanism of inhibition of horseradish peroxidase by cyclopropanone hydrate J. Biol. Chem. 257 1982 6328 6332
    • (1982) J. Biol. Chem. , vol.257 , pp. 6328-6332
    • Wiseman, J.S.1    Nichols, J.S.2    Kolpak, M.X.3
  • 55
    • 33846525435 scopus 로고    scopus 로고
    • Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes
    • DOI 10.1016/j.freeradbiomed.2006.11.019, PII S089158490600757X
    • M.G. Bonini, A.G. Siraki, B.S. Atanassov, and R.P. Mason Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes Free Radic. Biol. Med. 42 2007 530 540 (Pubitemid 46162122)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.4 , pp. 530-540
    • Bonini, M.G.1    Siraki, A.G.2    Atanassov, B.S.3    Mason, R.P.4
  • 56
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: Superoxide production and heme degradation
    • E. Nagababu, and J.M. Rifkind Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation Biochemistry 39 2000 12503 12511
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    Rifkind, J.M.2
  • 59
    • 0010575540 scopus 로고
    • Ferric chloride-catalyzed activation of hydrogen peroxide for the demethylation of N,N-dimethylaniline, the epoxidation of olefins, and the oxidative cleavage of vicinal diols in acetonitrile: A reaction mimic for cytochrome P-450
    • DOI 10.1073/pnas.84.7.1731
    • H. Sugimoto, L. Spencer, and D.T. Sawyer Ferric chloride-catalyzed activation of hydrogen-peroxide for the demethylation of N, N-dimethylaniline, the epoxidation of olefins, and the oxidative cleavage of vicinal diols in acetonitrile-a reaction mimic for cytochrome-P-450 Proc. Natl Acad. Sci. U. S. A. 84 1987 1731 1733 (Pubitemid 17054087)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.7 , pp. 1731-1733
    • Sugimoto, H.1    Spencer, L.2    Sawyer, D.T.3
  • 60
    • 33845557435 scopus 로고
    • High-valent iron-porphyrin complexes related to peroxidase and cytochrome P-450
    • J.T. Groves, R.C. Haushalter, M. Nakamura, T.E. Nemo, and B.J. Evans High-valent iron-porphyrin complexes related to peroxidase and cytochrome P-450 J. Am. Chem. Soc. 103 1981 2884 2886
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 2884-2886
    • Groves, J.T.1    Haushalter, R.C.2    Nakamura, M.3    Nemo, T.E.4    Evans, B.J.5
  • 61
    • 77956253312 scopus 로고    scopus 로고
    • Iron-mediated oxidation induces conformational changes within the redox-sensing protein HbpS
    • D. Ortiz de Orue Lucana, M. Roscher, A. Honigmann, J. Schwarz, Iron-mediated oxidation induces conformational changes within the redox-sensing protein HbpS. J. Biol. Chem. 285:28086-28096; 2010.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28086-28096
    • Lucana Orue De D.Ortiz1    Roscher, M.2    Honigmann, A.3    Schwarz, J.4
  • 63
    • 67649807405 scopus 로고    scopus 로고
    • Direct magnetic resonance evidence for peroxymonocarbonate involvement in the Cu,Zn-superoxide dismutase peroxidase catalytic cycle
    • M.G. Bonini, S.A. Gabel, K. Ranguelova, K. Stadler, E.F. Derose, R.E. London, and R.P. Mason Direct magnetic resonance evidence for peroxymonocarbonate involvement in the Cu,Zn-superoxide dismutase peroxidase catalytic cycle J. Biol. Chem. 284 2009 14618 14627
    • (2009) J. Biol. Chem. , vol.284 , pp. 14618-14627
    • Bonini, M.G.1    Gabel, S.A.2    Ranguelova, K.3    Stadler, K.4    Derose, E.F.5    London, R.E.6    Mason, R.P.7
  • 64
    • 0141905917 scopus 로고    scopus 로고
    • Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
    • DOI 10.1042/BJ20030685
    • A.L.P. Chapman, C.C. Winterbourn, S.O. Brennan, T.W. Jordan, and A.J. Kettle Characterization of non-covalent oligomers of proteins treated with hypochlorous acid Biochem. J. 375 2003 33 40 (Pubitemid 37255379)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 33-40
    • Chapman, A.L.P.1    Winterbourn, C.C.2    Brennan, S.O.3    Jordan, T.W.4    Kettle, A.J.5
  • 65
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • DOI 10.1021/tx960133r
    • E.R. Stadtman, and B.S. Berlett Reactive oxygen-mediated protein oxidation in aging and disease Chem. Res. Toxicol. 10 1997 485 494 (Pubitemid 27217204)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 66
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • DOI 10.1172/JCI200216781
    • A. Horwich Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions J. Clin. Invest. 110 2002 1221 1232 (Pubitemid 35285746)
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.9 , pp. 1221-1232
    • Horwich, A.1
  • 67
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DOI 10.1126/science.277.5334.1990
    • M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1997 1990 1993 (Pubitemid 27449140)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 69
    • 0028940342 scopus 로고
    • Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid
    • M.C. Vissers, and C.C. Winterbourn Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid Biochem. J. 307 Pt 1 1995 57 62
    • (1995) Biochem. J. , vol.307 , Issue.PART 1 , pp. 57-62
    • Vissers, M.C.1    Winterbourn, C.C.2
  • 70
    • 73549114427 scopus 로고    scopus 로고
    • Role of the membrane in the formation of heme degradation products in red blood cells
    • E. Nagababu, J.G. Mohanty, S. Bhamidipaty, G.R. Ostera, and J.M. Rifkind Role of the membrane in the formation of heme degradation products in red blood cells Life Sci. 86 2010 133 138
    • (2010) Life Sci. , vol.86 , pp. 133-138
    • Nagababu, E.1    Mohanty, J.G.2    Bhamidipaty, S.3    Ostera, G.R.4    Rifkind, J.M.5
  • 71
    • 44649126828 scopus 로고    scopus 로고
    • Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease
    • E. Nagababu, M.E. Fabry, R.L. Nagel, and J.M. Rifkind Heme degradation and oxidative stress in murine models for hemoglobinopathies: thalassemia, sickle cell disease and hemoglobin C disease Blood Cells Mol. Dis. 41 2008 60 66
    • (2008) Blood Cells Mol. Dis. , vol.41 , pp. 60-66
    • Nagababu, E.1    Fabry, M.E.2    Nagel, R.L.3    Rifkind, J.M.4
  • 72
    • 69249244191 scopus 로고    scopus 로고
    • Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase
    • I. Sliskovic, I. Abdulhamid, M. Sharma, and H.M. Abu-Soud Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase Free Radic. Biol. Med. 47 2009 1005 1013
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1005-1013
    • Sliskovic, I.1    Abdulhamid, I.2    Sharma, M.3    Abu-Soud, H.M.4
  • 73
    • 47249119192 scopus 로고    scopus 로고
    • Analysis of the mechanism by which melatonin inhibits human eosinophil peroxidase
    • DOI 10.1038/bjp.2008.173, PII BJP2008173
    • T. Lu, S. Galijasevic, I. Abdulhamid, and H.M. Abu-Soud Analysis of the mechanism by which melatonin inhibits human eosinophil peroxidase Br. J. Pharmacol. 154 2008 1308 1317 (Pubitemid 351992053)
    • (2008) British Journal of Pharmacology , vol.154 , Issue.6 , pp. 1308-1317
    • Lu, T.1    Galijasevic, S.2    Abdulhamid, I.3    Abu-Soud, H.M.4
  • 74
    • 39749093786 scopus 로고    scopus 로고
    • Melatonin is a potent inhibitor for myeloperoxidase
    • DOI 10.1021/bi702016q
    • S. Galijasevic, I. Abdulhamid, and H.M. Abu-Soud Melatonin is a potent inhibitor for myeloperoxidase Biochemistry 47 2008 2668 2677 (Pubitemid 351304572)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2668-2677
    • Galijasevic, S.1    Abdulhamid, I.2    Abu-Soud, H.M.3
  • 75
    • 41149090064 scopus 로고    scopus 로고
    • Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase
    • S. Galijasevic, I. Abdulhamid, and H.M. Abu-Soud Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase Free Radic. Biol. Med. 44 2008 1570 1577
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1570-1577
    • Galijasevic, S.1    Abdulhamid, I.2    Abu-Soud, H.M.3


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