메뉴 건너뛰기




Volumn 1814, Issue 4, 2011, Pages 480-486

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Author keywords

Electron transfer; Glutathione; Human myoglobin; Hydrogen peroxide; Thiyl radical

Indexed keywords

ALANINE; CYSTEINE; GLUTATHIONE; HYDROGEN PEROXIDE; MYOGLOBIN; RADICAL; REDUCING AGENT;

EID: 79952489454     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.01.008     Document Type: Article
Times cited : (9)

References (35)
  • 2
    • 0025289622 scopus 로고
    • X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution
    • S.R. Hubbard, W.A. Hendrickson, D.G. Lambright, S.G. Boxer, X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution, J. Mol. Biol. 213 (1990) 215-218.
    • (1990) J. Mol. Biol. , vol.213 , pp. 215-218
    • Hubbard, S.R.1    Hendrickson, W.A.2    Lambright, D.G.3    Boxer, S.G.4
  • 4
    • 0035830832 scopus 로고    scopus 로고
    • Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen
    • P.K. Witting, D.J. Douglas, A.G. Mauk, Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen, J. Biol. Chem. 276 (2001) 3991-3998.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3991-3998
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3
  • 5
    • 23044499916 scopus 로고    scopus 로고
    • Heme reduction by intramolecular electron transfer in cysteine mutant myoglobin under carbon monoxide atmosphere
    • DOI 10.1021/bi0507581
    • S. Hirota, K. Azuma, M. Fukuba, S. Kuroiwa, N. Funasaki, Heme reduction by intramolecular electron transfer in cysteine mutant myoglobin under carbon monoxide atmosphere, Biochemistry 44 (2005) 10322-10327. (Pubitemid 41076827)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10322-10327
    • Hirota, S.1    Azuma, K.2    Fukuba, M.3    Kuroiwa, S.4    Funasaki, N.5
  • 6
    • 53849095181 scopus 로고    scopus 로고
    • Myoglobin modification by enzyme-generated dopamine reactive species
    • S. Nicolis, M. Zucchelli, E. Monzani, L. Casella, Myoglobin modification by enzyme-generated dopamine reactive species, Chemistry 14 (2008) 8661-8673.
    • (2008) Chemistry , vol.14 , pp. 8661-8673
    • Nicolis, S.1    Zucchelli, M.2    Monzani, E.3    Casella, L.4
  • 7
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • P. George, D.H. Irvine, The reaction between metmyoglobin and hydrogen peroxide, Biochem. J. 52 (1952) 511-517.
    • (1952) Biochem. J. , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 8
    • 33748392625 scopus 로고
    • Free radical produced in the reaction of metmyoglobin with hydrogen peroxide
    • J.F. Gibson, D.J. Ingram, P. Nicholls, Free radical produced in the reaction of metmyoglobin with hydrogen peroxide, Nature 181 (1958) 1398-1399.
    • (1958) Nature , vol.181 , pp. 1398-1399
    • Gibson, J.F.1    Ingram, D.J.2    Nicholls, P.3
  • 9
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • N.K. King, M.E. Winfield, The mechanism of metmyoglobin oxidation, J. Biol. Chem. 238 (1963) 1520-1528.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • King, N.K.1    Winfield, M.E.2
  • 10
    • 0022273861 scopus 로고
    • Expoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface
    • P.R. Ortiz de Montellano, C.E. Catalano, Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface, J. Biol. Chem. 260 (1985) 9265-9271. (Pubitemid 16238308)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.16 , pp. 9265-9271
    • De Ortiz, M.P.R.1    Catalano, C.E.2
  • 11
    • 0026793349 scopus 로고
    • Intramolecular translocation of the protein radical formed in the reaction of recombinant sperm whale myoglobin with H2O2
    • A. Wilks, P.R. Ortiz de Montellano, Intramolecular translocation of the protein radical formed in the reaction of recombinant sperm whale myoglobin with H2O2, J. Biol. Chem. 267 (1992) 8827-8833.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8827-8833
    • Wilks, A.1    Ortiz De Montellano, P.R.2
  • 12
    • 0027509149 scopus 로고
    • The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin
    • S.I. Rao, A. Wilks, P.R. Ortiz de Montellano, The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin, J. Biol. Chem. 268 (1993) 803-809. (Pubitemid 23019706)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 803-809
    • Rao, S.I.1    Wilks, A.2    De Ortiz, M.P.R.3
  • 13
    • 0028360918 scopus 로고
    • Ferrylmyoglobin: Formation and chemical reactivity toward electron-donating compounds
    • C. Giulivi, E. Cadenas, Ferrylmyoglobin: formation and chemical reactivity toward electron-donating compounds, Meth. Enzymol. 233 (1994) 189-202.
    • (1994) Meth. Enzymol. , vol.233 , pp. 189-202
    • Giulivi, C.1    Cadenas, E.2
  • 14
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen-peroxide forms a peroxyl radical which oxidizes substrates
    • D.J. Kelman, J.A. Degray, R.P. Mason, Reaction of myoglobin with hydrogen-peroxide forms a peroxyl radical which oxidizes substrates, J. Biol. Chem. 269 (1994) 7458-7463.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    Degray, J.A.2    Mason, R.P.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 (2000) 20391-20398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20391-20398
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3
  • 16
    • 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 (2001) 16540-16547.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16540-16547
    • Witting, P.K.1    Mauk, A.G.2
  • 17
  • 18
    • 0023019698 scopus 로고
    • One- and two-electron oxidation of reduced glutathione by peroxidases
    • L.S. Harman, D.K. Carver, J. Schreiber, R.P. Mason, One- and two-electron oxidation of reduced glutathione by peroxidases, J. Biol. Chem. 261 (1986) 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
  • 19
    • 0037093679 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spin trapping investigation into the kinetics of glutathione oxidation by the superoxide radical: Re-evaluation of the rate constant
    • DOI 10.1016/S0891-5849(02)00791-8, PII S0891584902007918
    • C.M. Jones, A. Lawrence, P. Wardman, M.J. Burkitt, Electron paramagnetic resonance spin trapping investigation into the kinetics of glutathione oxidation by the superoxide radical: re-evaluation of the rate constant, Free Radic. Biol. Med. 32 (2002) 982-990. (Pubitemid 34465650)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.10 , pp. 982-990
    • Jones, C.M.1    Lawrence, A.2    Wardman, P.3    Burkitt, M.J.4
  • 21
    • 0032514904 scopus 로고    scopus 로고
    • The fate of the oxidizing tyrosyl radical in the presence of glutathione and ascorbate. Implications for the radical sink hypothesis
    • B.E. Sturgeon, H.J. Sipe Jr., D.P. Barr, J.T. Corbett, J.G. Martinez, R.P.Mason, The fate of the oxidizing tyrosyl radical in the presence of glutathione and ascorbate. Implications for the radical sink hypothesis, J. Biol. Chem. 273 (1998) 30116-30121.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30116-30121
    • Sturgeon, B.E.1    Sipe Jr., H.J.2    Barr, D.P.3    Corbett, J.T.4    Martinez, J.G.5    Mason, R.P.6
  • 22
    • 0018320433 scopus 로고
    • Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases
    • A. Wahllander, S. Soboll, H. Sies, I. Linke, M. Muller, Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases, FEBS Lett. 97 (1979) 138-140.
    • (1979) FEBS Lett. , vol.97 , pp. 138-140
    • Wahllander, A.1    Soboll, S.2    Sies, H.3    Linke, I.4    Muller, M.5
  • 25
    • 0022521858 scopus 로고
    • Neutrophil-endothelial cell interaction. Evidence for and mechanisms of the self-protection of bovine microvascular endothelial cells from hydrogen peroxide-induced oxidative stress
    • A. Dobrina, P. Patriarca, Neutrophil-endothelial cell interaction. Evidence for and mechanisms of the self-protection of bovine microvascular endothelial cells from hydrogen peroxide-induced oxidative stress, J. Clin. Invest. 78 (1986) 462-471. (Pubitemid 16074084)
    • (1986) Journal of Clinical Investigation , vol.78 , Issue.2 , pp. 462-471
    • Dobrina, A.1    Patriarca, P.2
  • 26
    • 0037167618 scopus 로고    scopus 로고
    • Role of tyrosine-103 in myoglobin peroxidase activity: Kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H2O2
    • P.K. Witting, A.G. Mauk, P.A. Lay, Role of tyrosine-103 in myoglobin peroxidase activity: kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H2O2, Biochemistry 41 (2002) 11495-11503.
    • (2002) Biochemistry , vol.41 , pp. 11495-11503
    • Witting, P.K.1    Mauk, A.G.2    Lay, P.A.3
  • 27
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • M.J. Davies, The oxidative environment and protein damage, Biochim. Biophys. Acta 1703 (2005) 93-109.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 28
    • 47049096866 scopus 로고    scopus 로고
    • Mechanisms of protein damage induced by cysteine thiyl radical formation
    • DOI 10.1021/tx800005u
    • C. Schoneich, Mechanisms of protein damage induced by cysteine thiyl radical formation, Chem. Res. Toxicol. 21 (2008) 1175-1179. (Pubitemid 351967380)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.6 , pp. 1175-1179
    • Schoneich, C.1
  • 29
    • 14644415062 scopus 로고    scopus 로고
    • Autoreduction of Ferryl Myoglobin: Discrimination among the Three Tyrosine and Two Tryptophan Residues as Electron Donors
    • DOI 10.1021/bi036241b
    • O.M. Lardinois, P.R. Ortiz de Montellano, Autoreduction of ferryl myoglobin: discrimination among the three tyrosine and two tryptophan residues as electron donors, Biochemistry 43 (2004) 4601-4610. (Pubitemid 38500589)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4601-4610
    • Lardinois, O.M.1    Ortiz, D.M.P.R.2
  • 31
    • 0023760002 scopus 로고
    • Thiol peroxyl radical formation from the reaction of cysteine thiyl radical with molecular oxygen: An ESR investigation
    • M.D. Sevilla, M.Y. Yan, D. Becker, Thiol peroxyl radical formation from the reaction of cysteine thiyl radical with molecular oxygen: an ESR investigation, Biochem. Biophys. Res. Commun. 155 (1988) 405-410.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 405-410
    • Sevilla, M.D.1    Yan, M.Y.2    Becker, D.3
  • 33
    • 0024517613 scopus 로고
    • Glutathione-dependent reduction of peroxides during ferryl- and met-myoglobin interconversion: A potential protective mechanism in muscle
    • DOI 10.1016/0891-5849(89)90039-7
    • D. Galaris, E. Cadenas, P. Hochstein, Glutathione-dependent reduction of peroxides during ferryl- and met-myoglobin interconversion: a potential protective mechanism in muscle, Free Radic. Biol. Med. 6 (1989) 473-478. (Pubitemid 19113578)
    • (1989) Free Radical Biology and Medicine , vol.6 , Issue.5 , pp. 473-478
    • Galaris, D.1    Cadenas, E.2    Hochstein, P.3
  • 34
    • 0037015996 scopus 로고    scopus 로고
    • EPR detection of glutathiyl and hemoglobin-cysteinyl radicals during the interaction of peroxynitrite with human erythrocytes
    • DOI 10.1021/bi0262202
    • O. Augusto, S. Lopes de Menezes, E. Linares, N. Romero, R. Radi, A. Denicola, EPR detection of glutathiyl and hemoglobin-cysteinyl radicals during the interaction of peroxynitrite with human erythrocytes, Biochemistry 41 (2002) 14323-14328. (Pubitemid 35403353)
    • (2002) Biochemistry , vol.41 , Issue.48 , pp. 14323-14328
    • Augusto, O.1    De Menezes, S.L.2    Linares, E.3    Romero, N.4    Radi, R.5    Denicola, A.6
  • 35
    • 0024309382 scopus 로고
    • Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link
    • C.E. Catalano, Y.S. Choe, P.R. Ortiz de Montellano, Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link, J. Biol. Chem. 264 (1989) 10534-10541. (Pubitemid 19161620)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10534-10541
    • Catalano, C.E.1    Choe, Y.S.2    Ortiz, D.M.P.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.