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Volumn 83, Issue 5, 2002, Pages 2845-2855

Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide

Author keywords

[No Author keywords available]

Indexed keywords

HEME; HEMOGLOBIN; HYDROGEN PEROXIDE; METHEMOGLOBIN; METMYOGLOBIN; MYOGLOBIN; PHENYLALANINE; TYROSINE; FREE RADICAL; IRON;

EID: 0036840513     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75293-4     Document Type: Article
Times cited : (75)

References (36)
  • 1
    • 0001459583 scopus 로고
    • Hemoglobin and myoglobin in their reactions with ligands
    • North-Holland, Amsterdam
    • Antonini, E., and M. Brunori. 1971. Hemoglobin and myoglobin in their reactions with ligands. Frontiers of Biology. North-Holland, Amsterdam.
    • (1971) Frontiers of Biology
    • Antonini, E.1    Brunori, M.2
  • 2
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • Barry, B. A., and G. T. Babcock. 1987. Tyrosine radicals are involved in the photosynthetic oxygen-evolving system. Proc. Natl. Acad. Sci. U.S.A. 84:7099-7103.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 3
    • 0025201528 scopus 로고
    • Tyrosine radicals in photosystem II and related model compounds: Characterization by isotopic labeling and EPR spectroscopy
    • Barry, B. A., M. K. el-Deeb, P. O. Sandusky, and G. T. Babcock. 1990. Tyrosine radicals in photosystem II and related model compounds: Characterization by isotopic labeling and EPR spectroscopy. J. Biol. Chem. 265:20139-20146.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20139-20146
    • Barry, B.A.1    El-Deeb, M.K.2    Sandusky, P.O.3    Babcock, G.T.4
  • 4
    • 0014429411 scopus 로고
    • The electron structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives
    • Blumberg, W. E., J. Peisach, B. A. Wittenberg, and J. B. Wittenberg. 1968. The electron structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives. J. Biol. Chem. 243:1854-1862.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1854-1862
    • Blumberg, W.E.1    Peisach, J.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 5
    • 0024577376 scopus 로고
    • Effect of the hyperbaric oxygenation of animals and man on mitochondrial function in their tissues (based on EPR study data)
    • Burgova, E. N., A. F. Vanin, E. A. Demurov, and I. V. Proshina. 1989. Effect of the hyperbaric oxygenation of animals and man on mitochondrial function in their tissues (based on EPR study data). Izv. Akad. Nauk SSSR Ser. Biol. 2:191-197.
    • (1989) Izv. Akad. Nauk SSSR Ser. Biol. , vol.2 , pp. 191-197
    • Burgova, E.N.1    Vanin, A.F.2    Demurov, E.A.3    Proshina, I.V.4
  • 8
    • 0026558882 scopus 로고
    • Direct detection of a globin-derived radical in leghemoglobin treated with peroxides
    • Davies, M. J., and A. Puppo. 1992. Direct detection of a globin-derived radical in leghemoglobin treated with peroxides. Biochem. J. 281:197-201.
    • (1992) Biochem. J. , vol.281 , pp. 197-201
    • Davies, M.J.1    Puppo, A.2
  • 11
    • 0022411108 scopus 로고
    • Discrepancies among published amino acid sequences of soybean leghemoglobins: Experimental evidence against cultivar differences as the sources of the discrepancies
    • Fuchsman, W. H. 1985. Discrepancies among published amino acid sequences of soybean leghemoglobins: Experimental evidence against cultivar differences as the sources of the discrepancies. Arch. Biochem. Biophys. 243:454-460.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 454-460
    • Fuchsman, W.H.1
  • 12
    • 0000456698 scopus 로고
    • Location of free electrons in porphin ring complexes
    • Gibson, J. F., and D. J. E. Ingram. 1956. Location of free electrons in porphin ring complexes. Nature. 178:871-872.
    • (1956) Nature , vol.178 , pp. 871-872
    • Gibson, J.F.1    Ingram, D.J.E.2
  • 13
    • 33748392625 scopus 로고
    • Free radical produced in the reaction of metmyoglobin with hydrogen peroxide
    • Gibson, J. F., D. J. E. Ingram, and P. Nicholls. 1958. Free radical produced in the reaction of metmyoglobin with hydrogen peroxide. Nature. 181:1398-1399.
    • (1958) Nature , vol.181 , pp. 1398-1399
    • Gibson, J.F.1    Ingram, D.J.E.2    Nicholls, P.3
  • 14
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther, M. R., D. J. Kelman, J. T. Corbett, and R. P. Mason. 1995. Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J. Biol. Chem. 270:16075-16081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16075-16081
    • Gunther, M.R.1    Kelman, D.J.2    Corbett, J.T.3    Mason, R.P.4
  • 18
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • Kelso King, N., and M. E. Winfield. 1963. The mechanism of metmyoglobin oxidation. J. Biol. Chem. 238:1520-1528.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • Kelso King, N.1    Winfield, M.E.2
  • 19
    • 0026620795 scopus 로고
    • High resolution crystal structures and comparisons of T state deoxyhaemoglobin and two liganded T-state haemoglobins: T(aoxy)haemoglobin and T(met)haemoglobin
    • Liddington, R., Z. Derewenda, E. Dodson, R. Hubbard, and G. Dodson. 1992. High resolution crystal structures and comparisons of T state deoxyhaemoglobin and two liganded T-state haemoglobins: T(aoxy)haemoglobin and T(met)haemoglobin. J. Mol. Biol. 228:551-579.
    • (1992) J. Mol. Biol. , vol.228 , pp. 551-579
    • Liddington, R.1    Derewenda, Z.2    Dodson, E.3    Hubbard, R.4    Dodson, G.5
  • 20
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in haemoglobin
    • McArthur, K. M., and M. J. Davies. 1993. Detection and reactions of the globin radical in haemoglobin. Biochim. Biophys. Acta. 1202:173-181.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 21
    • 0024788454 scopus 로고
    • Electron-spin resonance-spectrum of Tyr-151 free-radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium irridate
    • Miki, H., K. Harada, I. Yamazaki, M. Tamura, and H. Watanabe. 1989. Electron-spin resonance-spectrum of Tyr-151 free-radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium irridate. Arch. Biochem. Biophys. 275:354-362.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 354-362
    • Miki, H.1    Harada, K.2    Yamazaki, I.3    Tamura, M.4    Watanabe, H.5
  • 23
    • 33845377728 scopus 로고
    • The electron-spin resonance-spectrum of the tyrosyl radical
    • Sealy, R. C., L. Harman, P. R. West, and R. P. Mason. 1985. The electron-spin resonance-spectrum of the tyrosyl radical. J. Am. Chem. Soc. 107:3401-3406.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3401-3406
    • Sealy, R.C.1    Harman, L.2    West, P.R.3    Mason, R.P.4
  • 24
    • 0016616098 scopus 로고
    • Electron spin resonance study on peroxidase- and oxidase-reactions of horseradish peroxidase and methemoglobin
    • Shiga, T., and K. Imaizumi. 1975. Electron spin resonance study on peroxidase- and oxidase-reactions of horseradish peroxidase and methemoglobin. Arch. Biochem. Biophys. 167:469-479.
    • (1975) Arch. Biochem. Biophys. , vol.167 , pp. 469-479
    • Shiga, T.1    Imaizumi, K.2
  • 25
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A., and S. G. Sligar. 1987. High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 84:8961-8965.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 26
    • 33750692101 scopus 로고
    • Hindered internal rotation and ESR spectroscopy
    • Stone, E. W., and A. H. Maki. 1962. Hindered internal rotation and ESR spectroscopy. J. Chem. Phys. 37:1326-1333.
    • (1962) J. Chem. Phys. , vol.37 , pp. 1326-1333
    • Stone, E.W.1    Maki, A.H.2
  • 27
    • 0035820321 scopus 로고    scopus 로고
    • An EPR study of the peroxyl radicals induced by hydrogen peroxide in the heme proteins
    • Svistunenko, D. A. 2001. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the heme proteins. Biochim. Biophys. Acta. 1546:365-378.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 365-378
    • Svistunenko, D.A.1
  • 29
    • 0030896551 scopus 로고    scopus 로고
    • The globin-based free radical of ferryl hemoglobin is detected in normal human blood
    • Svistunenko, D. A., R. P. Patel, S. V. Voloshchenko, and M. T. Wilson. 1997b. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 272:7114-7121.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7114-7121
    • Svistunenko, D.A.1    Patel, R.P.2    Voloshchenko, S.V.3    Wilson, M.T.4
  • 30
    • 0029864259 scopus 로고    scopus 로고
    • An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction
    • Svistunenko, D. A., R. P. Patel, and M. T. Wilson. 1996. An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction. Free Radic. Res. 24:269-280.
    • (1996) Free Radic. Res. , vol.24 , pp. 269-280
    • Svistunenko, D.A.1    Patel, R.P.2    Wilson, M.T.3
  • 31
    • 0034132411 scopus 로고    scopus 로고
    • A new method for quantitation of spin concentration by EPR spectroscopy: Application to methemoglobin and metmyoglobin
    • Svistunenko, D. A., M. A. Sharpe, P. Nicholls, M. T. Wilson, and C. E. Cooper. 2000. A new method for quantitation of spin concentration by EPR spectroscopy: Application to methemoglobin and metmyoglobin. J. Magn. Reson. 142:266-275.
    • (2000) J. Magn. Reson. , vol.142 , pp. 266-275
    • Svistunenko, D.A.1    Sharpe, M.A.2    Nicholls, P.3    Wilson, M.T.4    Cooper, C.E.5
  • 32
    • 0013850651 scopus 로고
    • Changes in electron spin resonance signals of rat liver during chemical carcinogenesis
    • Vithayathil, A. J., J. L. Ternberg, and B. Commoner. 1965. Changes in electron spin resonance signals of rat liver during chemical carcinogenesis. Nature. 207:1246-1249.
    • (1965) Nature , vol.207 , pp. 1246-1249
    • Vithayathil, A.J.1    Ternberg, J.L.2    Commoner, B.3
  • 33
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • Vojtechovsky, J., K. Chu, J. Berendzen, R. M. Sweet, and I. Schlichting. 1999. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77:2153-2174.
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.M.4    Schlichting, I.5
  • 34
    • 0000787972 scopus 로고
    • Structure of the Y-D tyrosine radical in photosystem-II as revealed by H-2 electron-spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions
    • Warncke, K., G. T. Babcock, and J. McCracken. 1994. Structure of the Y-D tyrosine radical in photosystem-II as revealed by H-2 electron-spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions. J. Am. Chem. Soc. 116:7332-7340.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7332-7340
    • Warncke, K.1    Babcock, G.T.2    McCracken, J.3


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