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Volumn 410, Issue 3, 2008, Pages 565-574

Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links

Author keywords

EPR spectroscopy; Horseradish peroxidase (HRP); Myoglobin; Myosin; Protein oxidation; Radical

Indexed keywords

DISEASES; OXIDATION; OXIDATIVE STRESS; PARAMAGNETIC RESONANCE;

EID: 41149156956     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071107     Document Type: Article
Times cited : (110)

References (53)
  • 1
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. 1. General aspects
    • Davies, K. J. A. (1987) Protein damage and degradation by oxygen radicals. 1. General aspects. J. Biol. Chem. 262, 9895-9901
    • (1987) J. Biol. Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 2
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T., Fu, S. L., Stocker, R. and Davies, M. J. (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324, 1-18
    • (1997) Biochem. J , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.L.2    Stocker, R.3    Davies, M.J.4
  • 5
    • 0000915922 scopus 로고
    • Chemical, physical, and functional-properties of oxidized turkey white muscle myofibrillar proteins
    • Decker, E. A., Xiong, Y. L., Calvert, J. T., Crum, A. D. and Blanchard, S. P. (1993) Chemical, physical, and functional-properties of oxidized turkey white muscle myofibrillar proteins. J. Agric. Food Chem. 41, 186-189
    • (1993) J. Agric. Food Chem , vol.41 , pp. 186-189
    • Decker, E.A.1    Xiong, Y.L.2    Calvert, J.T.3    Crum, A.D.4    Blanchard, S.P.5
  • 6
    • 0029257253 scopus 로고
    • 2-generated myoglobin radical in cross-linking of myosin
    • 2-generated myoglobin radical in cross-linking of myosin. Free Radical Res. 22, 215-227
    • (1995) Free Radical Res , vol.22 , pp. 215-227
    • Hanan, T.1    Shaklai, N.2
  • 7
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu, G. and Xiong, Y. L. (2000) Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. J. Agric. Food Chem. 48, 624-630
    • (2000) J. Agric. Food Chem , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 8
    • 0032523796 scopus 로고    scopus 로고
    • Effect of oxygen free radicals on myosin in muscle fibres
    • Konczol, F., Lorinczy, D. and Belagyi, J. (1998) Effect of oxygen free radicals on myosin in muscle fibres. FEBS Lett. 427, 341-344
    • (1998) FEBS Lett , vol.427 , pp. 341-344
    • Konczol, F.1    Lorinczy, D.2    Belagyi, J.3
  • 10
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • George, P. and Irvine, D. H. (1952) The reaction between metmyoglobin and hydrogen peroxide. Biochem. J. 52, 511-517
    • (1952) Biochem. J , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 12
    • 0024309382 scopus 로고
    • Reactions of the protein radical in peroxide-treated myoglobin
    • Catalano, C. E., Choe, Y. S. and Ortiz de Montellano, P. R. (1989) Reactions of the protein radical in peroxide-treated myoglobin. J. Biol. Chem. 264, 10534-10541
    • (1989) J. Biol. Chem , vol.264 , pp. 10534-10541
    • Catalano, C.E.1    Choe, Y.S.2    Ortiz de Montellano, P.R.3
  • 15
    • 0034617045 scopus 로고    scopus 로고
    • 2. Involvement of a thiyl radical produced at cysteine 110
    • 2. Involvement of a thiyl radical produced at cysteine 110. J. Biol. Chem. 275, 20391-20398
    • (2000) J. Biol. Chem , vol.275 , pp. 20391-20398
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3
  • 16
    • 0033080051 scopus 로고    scopus 로고
    • Myoglobin-induced oxidative damage: Evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants
    • Irwin, J. A., Ostdal, H. and Davies, M. J. (1999) Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Arch. Biochem. Biophys. 362, 94-104
    • (1999) Arch. Biochem. Biophys , vol.362 , pp. 94-104
    • Irwin, J.A.1    Ostdal, H.2    Davies, M.J.3
  • 18
    • 0033080372 scopus 로고    scopus 로고
    • Formation of long-lived radicals on proteins by radical transfer from heme enzymes - a common process?
    • Ostdal, H., Andersen, H. J. and Davies, M. J. (1999) Formation of long-lived radicals on proteins by radical transfer from heme enzymes - a common process? Arch. Biochem. Biophys. 362, 105-112
    • (1999) Arch. Biochem. Biophys , vol.362 , pp. 105-112
    • Ostdal, H.1    Andersen, H.J.2    Davies, M.J.3
  • 21
    • 0037218503 scopus 로고    scopus 로고
    • Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima fatty (Oletf) rat
    • Oh-Ishi, M., Ueno, T. and Maeda, T. (2003) Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima fatty (Oletf) rat. Free Radical Biol. Med. 34, 11-22
    • (2003) Free Radical Biol. Med , vol.34 , pp. 11-22
    • Oh-Ishi, M.1    Ueno, T.2    Maeda, T.3
  • 23
    • 17044378603 scopus 로고    scopus 로고
    • Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems
    • White, M. Y., Cordwell, S. J., McCarron, H. C. K., Prasan, A. M., Craft, G., Hambly, B. D. and Jeremy, R. W. (2005) Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems. Proteomics 5, 1395-1410
    • (2005) Proteomics , vol.5 , pp. 1395-1410
    • White, M.Y.1    Cordwell, S.J.2    McCarron, H.C.K.3    Prasan, A.M.4    Craft, G.5    Hambly, B.D.6    Jeremy, R.W.7
  • 24
    • 33845590880 scopus 로고    scopus 로고
    • Proteomics of ischemia and reperfusion injuries in rabbit myocardium with and without intervention by an oxygen-free radical scavenger
    • White, M. Y., Tchen, A. S., McCarron, H. C. K., Hambly, B. D., Jeremy, R. W. and Cordwell, S. J. (2006) Proteomics of ischemia and reperfusion injuries in rabbit myocardium with and without intervention by an oxygen-free radical scavenger. Proteomics 6, 6221-6233
    • (2006) Proteomics , vol.6 , pp. 6221-6233
    • White, M.Y.1    Tchen, A.S.2    McCarron, H.C.K.3    Hambly, B.D.4    Jeremy, R.W.5    Cordwell, S.J.6
  • 25
    • 0032439806 scopus 로고    scopus 로고
    • Involvement of the oxygen storage protein myoglobin in muscle damage under oxidative stress
    • Kamin-Belsky, N., Tomashov, R., Arav, R. and Shaklai, N. (1998) Involvement of the oxygen storage protein myoglobin in muscle damage under oxidative stress. Adv. Exp. Med. Biol. 454, 219-223
    • (1998) Adv. Exp. Med. Biol , vol.454 , pp. 219-223
    • Kamin-Belsky, N.1    Tomashov, R.2    Arav, R.3    Shaklai, N.4
  • 26
    • 0028882867 scopus 로고
    • Peroxidative interaction of myoglobin and myosin
    • Hanan, T. and Shaklai, N. (1995) Peroxidative interaction of myoglobin and myosin. Eur. J. Biochem. 233, 930-936
    • (1995) Eur. J. Biochem , vol.233 , pp. 930-936
    • Hanan, T.1    Shaklai, N.2
  • 28
    • 84985275078 scopus 로고
    • Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation
    • Smith, D. M. (1987) Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation. J. Food Sci. 52, 22-27
    • (1987) J. Food Sci , vol.52 , pp. 22-27
    • Smith, D.M.1
  • 29
    • 0000989650 scopus 로고
    • Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein
    • Wan, L., Xiong, Y. L. and Decker, E. A. (1993) Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein. J. Agric. Food Chem. 41, 2267-2271
    • (1993) J. Agric. Food Chem , vol.41 , pp. 2267-2271
    • Wan, L.1    Xiong, Y.L.2    Decker, E.A.3
  • 30
    • 34547471557 scopus 로고    scopus 로고
    • High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage
    • Lund, M. N., Lametsch, R., Hviid, M. S., Jensen, O. N. and Skibsted, L. H. (2007) High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage. Meat Sci. 77, 295-303
    • (2007) Meat Sci , vol.77 , pp. 295-303
    • Lund, M.N.1    Lametsch, R.2    Hviid, M.S.3    Jensen, O.N.4    Skibsted, L.H.5
  • 31
    • 33745757012 scopus 로고    scopus 로고
    • Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems
    • Park, D., Xiong, Y. L., Alderton, A. L. and Ooizumi, T. (2006) Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems. J. Agric. Food Chem. 54, 4445-4451
    • (2006) J. Agric. Food Chem , vol.54 , pp. 4445-4451
    • Park, D.1    Xiong, Y.L.2    Alderton, A.L.3    Ooizumi, T.4
  • 32
    • 0014690148 scopus 로고
    • Pyrophosphate binding to and adenosine triphosphate activity of myosin and its proteolytic fragments
    • Nauss, K. M., Kitagawa, S. and Gergely, J. (1969) Pyrophosphate binding to and adenosine triphosphate activity of myosin and its proteolytic fragments. J. Biol. Chem. 244, 755-765
    • (1969) J. Biol. Chem , vol.244 , pp. 755-765
    • Nauss, K.M.1    Kitagawa, S.2    Gergely, J.3
  • 33
    • 0001226125 scopus 로고
    • Kinetics and mechanism of thermal oxidation and photooxidation of nitrosylmyoglobin in aqueous solution
    • Andersen, H. J. and Skibsted, L. H. (1992) Kinetics and mechanism of thermal oxidation and photooxidation of nitrosylmyoglobin in aqueous solution. J. Agric. Food Chem. 40, 1741-1750
    • (1992) J. Agric. Food Chem , vol.40 , pp. 1741-1750
    • Andersen, H.J.1    Skibsted, L.H.2
  • 35
    • 22344451993 scopus 로고    scopus 로고
    • Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus
    • Morgan, P. E., Sturgess, A. D. and Davies, M. J. (2005) Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus. Arthritis Rheum. 52, 2069-2079
    • (2005) Arthritis Rheum , vol.52 , pp. 2069-2079
    • Morgan, P.E.1    Sturgess, A.D.2    Davies, M.J.3
  • 36
    • 0029991419 scopus 로고    scopus 로고
    • Synthesis of peroxynitrite in a two-phase system using isoamyl nitrite and hydrogen peroxide
    • Uppu, R. M. and Pryor, W. A. (1996) Synthesis of peroxynitrite in a two-phase system using isoamyl nitrite and hydrogen peroxide. Anal. Biochem. 236, 242-249
    • (1996) Anal. Biochem , vol.236 , pp. 242-249
    • Uppu, R.M.1    Pryor, W.A.2
  • 37
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • Winterbourn, C. C. (1990) Oxidative reactions of hemoglobin. Methods Enzymol. 186, 265-272
    • (1990) Methods Enzymol , vol.186 , pp. 265-272
    • Winterbourn, C.C.1
  • 38
    • 0032143406 scopus 로고    scopus 로고
    • Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
    • Fu, S., Davies, M. J., Stocker, R. and Dean, R. T. (1998) Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque. Biochem. J. 333, 519-525
    • (1998) Biochem. J , vol.333 , pp. 519-525
    • Fu, S.1    Davies, M.J.2    Stocker, R.3    Dean, R.T.4
  • 39
    • 0026063955 scopus 로고
    • Identification of a globin-free radical in equine myoglobin treated with peroxides
    • Davies, M. J. (1991) Identification of a globin-free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta 1077, 86-90
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 86-90
    • Davies, M.J.1
  • 40
    • 27744494382 scopus 로고    scopus 로고
    • On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide
    • Cooper, C. E., Jurd, M., Nicholls, P., Wankasi, M. M., Svistuenko, D. A., Reeder, B. J. and Wilson, M. T. (2005) On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide. Dalton Trans. 21, 3483-3488
    • (2005) Dalton Trans , vol.21 , pp. 3483-3488
    • Cooper, C.E.1    Jurd, M.2    Nicholls, P.3    Wankasi, M.M.4    Svistuenko, D.A.5    Reeder, B.J.6    Wilson, M.T.7
  • 41
    • 0343035716 scopus 로고    scopus 로고
    • Density functional calculations on model tyrosyl radicals
    • Himo, F., Graslund, A. and Eriksson, L. A. (1997) Density functional calculations on model tyrosyl radicals. Biophys. J. 72, 1556-1567
    • (1997) Biophys. J , vol.72 , pp. 1556-1567
    • Himo, F.1    Graslund, A.2    Eriksson, L.A.3
  • 44
    • 0034062553 scopus 로고    scopus 로고
    • A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide
    • Gunther, M. R., Sturgeon, B. E. and Mason, R. P. (2000) A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Free Radical Biol. Med. 28, 709-719
    • (2000) Free Radical Biol. Med , vol.28 , pp. 709-719
    • Gunther, M.R.1    Sturgeon, B.E.2    Mason, R.P.3
  • 45
    • 0037090563 scopus 로고    scopus 로고
    • Identification of protein-derived tyrosyl radical in the reaction of cytochrome c and hydrogen peroxide: Characterization by ESR spin-trapping, HPLC and MS
    • Qian, S. Y., Chen, Y. R., Deterding, L. J., Fann, Y. C., Chignell, C. F., Tomer, K. B. and Mason, R. P. (2002) Identification of protein-derived tyrosyl radical in the reaction of cytochrome c and hydrogen peroxide: characterization by ESR spin-trapping, HPLC and MS. Biochem. J. 363, 281-288
    • (2002) Biochem. J , vol.363 , pp. 281-288
    • Qian, S.Y.1    Chen, Y.R.2    Deterding, L.J.3    Fann, Y.C.4    Chignell, C.F.5    Tomer, K.B.6    Mason, R.P.7
  • 46
    • 0033610818 scopus 로고    scopus 로고
    • Electron paramagnetic resonance detection of free tyrosyl radical generated by myeloperoxidase, lactoperoxidase, and horseradish peroxidase
    • McCormick, M. L., Gaut, J. P., Lin, T.-S., Britigan, B. E., Buettner, G. R. and Heinecke, J. W. (1998) Electron paramagnetic resonance detection of free tyrosyl radical generated by myeloperoxidase, lactoperoxidase, and horseradish peroxidase. J. Biol. Chem. 273, 32030-32037
    • (1998) J. Biol. Chem , vol.273 , pp. 32030-32037
    • McCormick, M.L.1    Gaut, J.P.2    Lin, T.-S.3    Britigan, B.E.4    Buettner, G.R.5    Heinecke, J.W.6
  • 47
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates
    • Kelman, D. J., De Gray, J. A. and Mason, R. P. (1994) Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. J. Biol. Chem. 269, 7458-7463
    • (1994) J. Biol. Chem , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    De Gray, J.A.2    Mason, R.P.3
  • 48
    • 0026558882 scopus 로고
    • Direct detection of a globin-derived radical in leghaemoglobin treated with peroxides
    • Davies, M. J. and Puppo, A. (1992) Direct detection of a globin-derived radical in leghaemoglobin treated with peroxides. Biochem. J. 281, 197-201
    • (1992) Biochem. J , vol.281 , pp. 197-201
    • Davies, M.J.1    Puppo, A.2
  • 49
    • 0026509008 scopus 로고
    • The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formation of thiyl radical intermediates
    • Romero, F. J., Ordonez, I., Arduini, A. and Cadenas, E. (1992) The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formation of thiyl radical intermediates. J. Biol. Chem. 267, 1680-1688
    • (1992) J. Biol. Chem , vol.267 , pp. 1680-1688
    • Romero, F.J.1    Ordonez, I.2    Arduini, A.3    Cadenas, E.4
  • 50
    • 0021329847 scopus 로고
    • Free radical metabolites of L-cysteine oxidation
    • Harman, L. S., Mottley, C. and Mason, R. P. (1984) Free radical metabolites of L-cysteine oxidation. J. Biol. Chem. 259, 5606-5611
    • (1984) J. Biol. Chem , vol.259 , pp. 5606-5611
    • Harman, L.S.1    Mottley, C.2    Mason, R.P.3
  • 51
    • 0023019698 scopus 로고
    • One- and two-electron oxidation of reduced glutathione by peroxidases
    • Harman, L. S., Carver, D. K., Schreiber, J. and Mason, R. P. (1986) One- and two-electron oxidation of reduced glutathione by peroxidases. J. Biol. Chem. 261, 1642-1648
    • (1986) J. Biol. Chem , vol.261 , pp. 1642-1648
    • Harman, L.S.1    Carver, D.K.2    Schreiber, J.3    Mason, R.P.4
  • 52
    • 0022938972 scopus 로고
    • Unpaired electron migration between aromatic and sulfur peptide units
    • Prutz, W. A., Butler, J., Land, E. J. and Swallow, A. J. (1986) Unpaired electron migration between aromatic and sulfur peptide units. Free Radical Res. Commun. 2, 69-75
    • (1986) Free Radical Res. Commun , vol.2 , pp. 69-75
    • Prutz, W.A.1    Butler, J.2    Land, E.J.3    Swallow, A.J.4
  • 53
    • 0019327137 scopus 로고
    • Direct demonstration of electron transfer between tryptophan and tyrosine in proteins
    • Prutz, W. A., Butler, J., Land, E. J. and Swallow, A. J. (1980) Direct demonstration of electron transfer between tryptophan and tyrosine in proteins. Biochem. Biophys. Res. Commun. 96, 408-414
    • (1980) Biochem. Biophys. Res. Commun , vol.96 , pp. 408-414
    • Prutz, W.A.1    Butler, J.2    Land, E.J.3    Swallow, A.J.4


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