메뉴 건너뛰기




Volumn 16, Issue 5, 2003, Pages 652-660

Tryptophan-14 is the preferred site of DBNBS spin trapping in the self-peroxidation reaction of sperm whale metmyoglobin with a single equivalent of hydrogen peroxide

Author keywords

[No Author keywords available]

Indexed keywords

3,5 DIBROMO 4 NITROSOBENZENESULFONIC ACID; AMINO ACID; CARBON 13; FREE RADICAL; HYDROGEN PEROXIDE; METMYOGLOBIN; PRONASE; SULFONIC ACID DERIVATIVE; TRYPTOPHAN DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0038243555     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0256580     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 0024300827 scopus 로고
    • Radicals in biological catalysis
    • Stubbe, J. (1988) Radicals in biological catalysis. Biochemistry 27, 3893-3900.
    • (1988) Biochemistry , vol.27 , pp. 3893-3900
    • Stubbe, J.1
  • 2
    • 0026091195 scopus 로고
    • Radical-induced damage to proteins: Esr spin-trapping studies
    • Davies, M. J., Gilbert, B. C., and Haywood, R. M. (1991) Radical-induced damage to proteins: esr spin-trapping studies. Free Radical Res. Commun. 15, 111-127.
    • (1991) Free Radical Res. Commun. , vol.15 , pp. 111-127
    • Davies, M.J.1    Gilbert, B.C.2    Haywood, R.M.3
  • 4
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther, M. R., Kelman, D. J., Corbett, J. T., and Mason, R. P. (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
  • 6
    • 0035844279 scopus 로고    scopus 로고
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical. J. Biol. Chem. 276, 1540-16547.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1540-16547
    • Witting, P.K.1    Mauk, A.G.2
  • 9
    • 0029900542 scopus 로고    scopus 로고
    • ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide
    • Barr, D. P., Gunther, M. R., Deterding, L. J., Tomer, K. B., and Mason, R. P. (1996) ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. J. Biol. Chem. 271, 15498-15503.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15498-15503
    • Barr, D.P.1    Gunther, M.R.2    Deterding, L.J.3    Tomer, K.B.4    Mason, R.P.5
  • 10
    • 0035877617 scopus 로고    scopus 로고
    • Mass spectral analysis of protein-based radicals using DBNBS. Nonradical adduct formation versus spin trapping
    • Filosa, A., and English, A. M. (2001) Mass spectral analysis of protein-based radicals using DBNBS. Nonradical adduct formation versus spin trapping. J. Biol. Chem. 276, 21022-21027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21022-21027
    • Filosa, A.1    English, A.M.2
  • 11
    • 0034671959 scopus 로고    scopus 로고
    • Direct evidence for apo B-100-mediated copper reduction: Studies with purified apo B-100 and detection of tryptophanyl radicals
    • Batthyany, C., Santos, C. X. C., Botti, H., Cervenansky, C., Radi, R., Augusto, O., and Rubbo, H. (2000) Direct evidence for apo B-100-mediated copper reduction: studies with purified apo B-100 and detection of tryptophanyl radicals. Arch. Biochem. Biophys. 384, 335-340.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 335-340
    • Batthyany, C.1    Santos, C.X.C.2    Botti, H.3    Cervenansky, C.4    Radi, R.5    Augusto, O.6    Rubbo, H.7
  • 13
    • 0033544871 scopus 로고    scopus 로고
    • Spin trapping and protein cross-linking of the lactoperoxidase protein radical
    • Lardinois, O. M., Medzihradszky, K. F., and Ortiz de Montellano, P. R. (1999) Spin trapping and protein cross-linking of the lactoperoxidase protein radical. J. Biol. Chem. 274, 35441-35448.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35441-35448
    • Lardinois, O.M.1    Medzihradszky, K.F.2    Ortiz de Montellano, P.R.3
  • 14
    • 0029010437 scopus 로고
    • Detection of protein radicals formed by the photodynamic action of porphyrin sensitizers
    • Silvester, J. A., Timmins, G. S., and Davies, M. J. (1995) Detection of protein radicals formed by the photodynamic action of porphyrin sensitizers. Biochem. Soc. Trans. 23, 261S.
    • (1995) Biochem. Soc. Trans. , vol.23
    • Silvester, J.A.1    Timmins, G.S.2    Davies, M.J.3
  • 15
    • 0031045361 scopus 로고    scopus 로고
    • Oxidative damage to collagen and related substrates by metal ion/hydrogen peroxide systems: Random attack or site-specific damage?
    • Hawkins, C. L., and Davies, M. J. (1997) Oxidative damage to collagen and related substrates by metal ion/hydrogen peroxide systems: random attack or site-specific damage? Biochim. Biophys. Acta 1360, 84-96.
    • (1997) Biochim. Biophys. Acta. , vol.1360 , pp. 84-96
    • Hawkins, C.L.1    Davies, M.J.2
  • 16
    • 0031045787 scopus 로고    scopus 로고
    • One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: Evidence for the formation of protein tryptophan-centred radicals
    • Pietraforte, D., and Minetti, M. (1997) One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centred radicals. Biochem. J. 321, 743-750.
    • (1997) Biochem. J. , vol.321 , pp. 743-750
    • Pietraforte, D.1    Minetti, M.2
  • 18
    • 0037088630 scopus 로고    scopus 로고
    • Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase
    • Gunther, M. R., Peters, J. A., and Sivaneri, M. K. (2002) Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase. J. Biol. Chem. 277, 9160-9166.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9160-9166
    • Gunther, M.R.1    Peters, J.A.2    Sivaneri, M.K.3
  • 19
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins, C. L., and Davies, M. J. (2001) Generation and propagation of radical reactions on proteins, Biochim. Biophys. Acta 1504, 196-219.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 20
    • 0036909376 scopus 로고    scopus 로고
    • Determining the site of spin-trapping of the equine myoglobin radical by combined use of EPR, electrophoretic purification, and mass spectrometry
    • Harris, M. N., Burchiel, S. W., Winyard, P. G., Engen, J. R., Mobarak, C. D., and Timmins, G. S. (2002) Determining the site of spin-trapping of the equine myoglobin radical by combined use of EPR, electrophoretic purification, and mass spectrometry. Chem. Res. Toxicol. 15, 1589-1594.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1589-1594
    • Harris, M.N.1    Burchiel, S.W.2    Winyard, P.G.3    Engen, J.R.4    Mobarak, C.D.5    Timmins, G.S.6
  • 21
    • 0032557672 scopus 로고    scopus 로고
    • Characterization of cytochrome c free radical reactions with peptides by mass spectrometry
    • Deterding, L. J., Barr, D. P., Mason, R. P., and Tomer, K. B. (1998) Characterization of cytochrome c free radical reactions with peptides by mass spectrometry. J. Biol. Chem. 273, 12863-12869.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12863-12869
    • Deterding, L.J.1    Barr, D.P.2    Mason, R.P.3    Tomer, K.B.4
  • 22
    • 0035933786 scopus 로고    scopus 로고
    • 2-mediated cross-linking between lactoperoxidase and myoglobin. Elucidation of protein-protein radical transfer reactions
    • 2-mediated cross-linking between lactoperoxidase and myoglobin. Elucidation of protein-protein radical transfer reactions. J. Biol. Chem. 276, 23186-23191.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23186-23191
    • Lardinois, O.M.1    Ortiz de Montellano, P.R.2
  • 23
    • 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
  • 24
    • 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
  • 25
    • 49049138188 scopus 로고
    • Charge transfer between tryptophan and tyrosine in proteins
    • Butler, J., Land, E. J., Prutz, W. A., and Swallow, A. J. (1982) Charge transfer between tryptophan and tyrosine in proteins. Biochim. Biophys. Acta 705, 150-162.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 150-162
    • Butler, J.1    Land, E.J.2    Prutz, W.A.3    Swallow, A.J.4
  • 26
    • 37049181402 scopus 로고
    • Long-range electron transfer in heme proteins
    • Mayo, S. L., Ellis, W. R., Crutchley, R. J., Jr., and Gray, H. B. (1986) Long-range electron transfer in heme proteins. Science 233, 948-952.
    • (1986) Science , vol.233 , pp. 948-952
    • Mayo, S.L.1    Ellis, W.R.2    Crutchley R.J., Jr.3    Gray, H.B.4
  • 27
    • 0027993949 scopus 로고
    • Characterization of a tyrosyl radical in prostaglandin endoperoxide synthase-2
    • Hsi, L. C., Hoganson, C. W., Babcock, G. T., and Smith, W. L. (1994) Characterization of a tyrosyl radical in prostaglandin endoperoxide synthase-2. Biochem. Biophys. Res. Commun. 202, 1592-1598.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1592-1598
    • Hsi, L.C.1    Hoganson, C.W.2    Babcock, G.T.3    Smith, W.L.4
  • 28
    • 0025888387 scopus 로고
    • Electron spin resonance investigation of tyrosyl radicals of prostaglandin H synthase. Relation to enzyme catalysis
    • Lassmann, G., Odenwaller, R., Curtis, J. F., DeGray, J. A., Mason, R. P., Marnett, L. J., and Eling, T. E. (1991) Electron spin resonance investigation of tyrosyl radicals of prostaglandin H synthase. Relation to enzyme catalysis. J. Biol. Chem. 266, 20045-20055.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20045-20055
    • Lassmann, G.1    Odenwaller, R.2    Curtis, J.F.3    DeGray, J.A.4    Mason, R.P.5    Marnett, L.J.6    Eling, T.E.7
  • 29
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • Bollinger, J. M., Jr., Edmondson, D. E., Huynh, B. H., Filley, J., Norton, J. R., and Stubbe, J. (1991) Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science 253, 292-298.
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger J.M., Jr.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, J.4    Norton, J.R.5    Stubbe, J.6
  • 30
    • 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
  • 34
    • 0028523532 scopus 로고
    • Appearance of ESR signals by the reaction of 3,5-dibromo-4-nitrosobenzene-sulfonate (DBNBS) and nonradical biological components
    • Hiramoto, K., Hasegawa, Y., and Kikugawa, K. (1994) Appearance of ESR signals by the reaction of 3,5-dibromo-4-nitrosobenzene-sulfonate (DBNBS) and nonradical biological components. Free Radical Res. 21, 341-349.
    • (1994) Free Radical Res. , vol.21 , pp. 341-349
    • Hiramoto, K.1    Hasegawa, Y.2    Kikugawa, K.3
  • 35
    • 0020490335 scopus 로고
    • Redox transformations in ferrimyoglobin induced by radiation-generated free radicals in aqueous solution
    • Whitburn, K. D., Shieh, J. J., Sellers, R. M., Hoffman, M. Z., and Taub, I. A. (1982) Redox transformations in ferrimyoglobin induced by radiation-generated free radicals in aqueous solution. J. Biol. Chem. 257, 1860-1869.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1860-1869
    • Whitburn, K.D.1    Shieh, J.J.2    Sellers, R.M.3    Hoffman, M.Z.4    Taub, I.A.5
  • 37
    • 0014473352 scopus 로고
    • Electron spin resonance of an irradiated single crystal of L-tyrosine-HCl
    • Fasanella, E. L., and Gordy, W. (1969) Electron spin resonance of an irradiated single crystal of L-tyrosine-HCl. Proc. Natl. Acad. Sci. U.S.A. 62, 299-304.
    • (1969) Proc. Natl. Acad. Sci. U.S.A. , vol.62 , pp. 299-304
    • Fasanella, E.L.1    Gordy, W.2
  • 38
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.