메뉴 건너뛰기




Volumn 6, Issue 6, 2004, Pages 954-966

The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology

Author keywords

[No Author keywords available]

Indexed keywords

FERRYLMYOGLOBIN; HEME OXYGENASE; HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN; PEROXIDASE; PEROXIDE; PSEUDOPEPTIDE;

EID: 7244243910     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2004.6.954     Document Type: Review
Times cited : (170)

References (97)
  • 1
    • 0342467554 scopus 로고
    • Reaction between lipid hydroperoxide and hemoglobin studied by a spectrophotoinetic and a spin trapping method
    • Aoshima H, Yoshida Y, and Taniguchi H. Reaction between lipid hydroperoxide and hemoglobin studied by a spectrophotoinetic and a spin trapping method. Agric Biol Chem 50: 1777-1783, 1986.
    • (1986) Agric Biol Chem , vol.50 , pp. 1777-1783
    • Aoshima, H.1    Yoshida, Y.2    Taniguchi, H.3
  • 2
    • 0025616146 scopus 로고
    • Detection of ferryl myoglobin in the isolated ischemic rat heart
    • Arduini A, Eddy L, and Hochstein P. Detection of ferryl myoglobin in the isolated ischemic rat heart. Free Radic Biol Med 9: 511-513, 1990.
    • (1990) Free Radic Biol Med , vol.9 , pp. 511-513
    • Arduini, A.1    Eddy, L.2    Hochstein, P.3
  • 3
    • 0015111355 scopus 로고
    • Intrarenal hemodynamics in glycerol-induced myohemoglobinuric acute renal failure in the rat
    • Ayer G, Grandchamp A, Wyler T, and Truniger B. Intrarenal hemodynamics in glycerol-induced myohemoglobinuric acute renal failure in the rat. Circ Res 29: 128-135, 1971.
    • (1971) Circ Res , vol.29 , pp. 128-135
    • Ayer, G.1    Grandchamp, A.2    Wyler, T.3    Truniger, B.4
  • 4
    • 0032558387 scopus 로고    scopus 로고
    • Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical
    • Balagopalakrishna C, Abugo OO, Horsky J, Manoharan PT, Nagababu E, and Rifkind JM. Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical. Biochemistry 37: 13194-13202, 1998.
    • (1998) Biochemistry , vol.37 , pp. 13194-13202
    • Balagopalakrishna, C.1    Abugo, O.O.2    Horsky, J.3    Manoharan, P.T.4    Nagababu, E.5    Rifkind, J.M.6
  • 5
    • 0029661490 scopus 로고    scopus 로고
    • Nitric oxide and blood pressure: Effects of nitric oxide deficiency
    • Baylis C and Vallance P. Nitric oxide and blood pressure: effects of nitric oxide deficiency. Curr Opin Nephrol Hypertens 5: 80-88, 1996.
    • (1996) Curr Opin Nephrol Hypertens , vol.5 , pp. 80-88
    • Baylis, C.1    Vallance, P.2
  • 7
    • 0019507299 scopus 로고
    • Electron spin resonance studies on normal human uterus and cervix and on benign and malignant uterine tumors
    • Benedetto C, Bocci A, Dianzani MU, Ghiringhello B, Slater TF, Tomasi A, and Vannini V. Electron spin resonance studies on normal human uterus and cervix and on benign and malignant uterine tumors. Cancer Res 41: 2936-2942, 1981.
    • (1981) Cancer Res , vol.41 , pp. 2936-2942
    • Benedetto, C.1    Bocci, A.2    Dianzani, M.U.3    Ghiringhello, B.4    Slater, T.F.5    Tomasi, A.6    Vannini, V.7
  • 8
    • 0037167576 scopus 로고    scopus 로고
    • Identification of oxidized derivatives of neuroketals
    • Bernoud-Hubac N and Roberts LJ 2nd. Identification of oxidized derivatives of neuroketals. Biochemistry 41: 11466-11471, 2002.
    • (2002) Biochemistry , vol.41 , pp. 11466-11471
    • Bernoud-Hubac, N.1    Roberts II, L.J.2
  • 9
    • 0035903163 scopus 로고    scopus 로고
    • Formation of highly reactive gamma-ketoaldehydes (neuroketals) as products of the neuroprostane pathway
    • Bernoud-Hubac N, Davies SS, Boutaud O, Montine TJ, and Roberts LJ 2nd. Formation of highly reactive gamma-ketoaldehydes (neuroketals) as products of the neuroprostane pathway. J Biol Chem 276: 30964-30970, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 30964-30970
    • Bernoud-Hubac, N.1    Davies, S.S.2    Boutaud, O.3    Montine, T.J.4    Roberts II, L.J.5
  • 10
    • 0025712626 scopus 로고
    • Early management of shock and prophylaxis of acute renal failure in traumatic rhabdomyolysis
    • Better OS and Stein JH. Early management of shock and prophylaxis of acute renal failure in traumatic rhabdomyolysis. N Engl J Med 322: 825-829, 1990.
    • (1990) N Engl J Med , vol.322 , pp. 825-829
    • Better, O.S.1    Stein, J.H.2
  • 11
    • 0024309382 scopus 로고
    • Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link
    • Catalano CE, Choe YS, and Ortiz de Montellano PR. Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link. J Biol Chem 264: 10534-10541, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 10534-10541
    • Catalano, C.E.1    Choe, Y.S.2    Ortiz De Montellano, P.R.3
  • 13
    • 0026063955 scopus 로고
    • Identification of a globin free-radical in equine myoglobin treated with peroxides
    • Davies MJ. Identification of a globin free-radical in equine myoglobin treated with peroxides. Biochim Biophys Acta 1077: 86-90, 1991.
    • (1991) Biochim Biophys Acta , vol.1077 , pp. 86-90
    • Davies, M.J.1
  • 14
    • 0026558882 scopus 로고
    • Direct detection of a globin-derived radical in leghemoglobin treated with peroxides
    • Davies MJ and Puppo A. Direct detection of a globin-derived radical in leghemoglobin treated with peroxides. Biochem J 281: 197-201, 1992.
    • (1992) Biochem J , vol.281 , pp. 197-201
    • Davies, M.J.1    Puppo, A.2
  • 15
    • 0036583274 scopus 로고    scopus 로고
    • Effects of reactive gamma-ketoaldehydes formed by the isoprostane pathway (isoketals) and cyclooxygenase pathway (levuglandins) on proteasome function
    • Davies SS, Amarnath V, Montine KS, Bernoud-Hubac N, Boutaud O, Montine TJ, and Roberts LJ 2nd. Effects of reactive gamma-ketoaldehydes formed by the isoprostane pathway (isoketals) and cyclooxygenase pathway (levuglandins) on proteasome function. FASEB J 16: 715-717, 2002.
    • (2002) FASEB J , vol.16 , pp. 715-717
    • Davies, S.S.1    Amarnath, V.2    Montine, K.S.3    Bernoud-Hubac, N.4    Boutaud, O.5    Montine, T.J.6    Roberts II, L.J.7
  • 17
    • 0031801111 scopus 로고    scopus 로고
    • Recovery and rehabilitation following subarachnoid haemorrhage. Part I: Outcome after inpatient rehabilitation
    • Dombovy ML, Drew-Cates J, and Serdans R. Recovery and rehabilitation following subarachnoid haemorrhage. Part I: Outcome after inpatient rehabilitation. Brain Inj 12: 443-454, 1998.
    • (1998) Brain Inj , vol.12 , pp. 443-454
    • Dombovy, M.L.1    Drew-Cates, J.2    Serdans, R.3
  • 18
    • 0017281663 scopus 로고
    • The steady-state kinetics of the oxygenation of linoleic acid catalysed by soybean lipoxygenase
    • Egmond MR, Brunori M, and Fasella PM. The steady-state kinetics of the oxygenation of linoleic acid catalysed by soybean lipoxygenase. Eur J Biochem 61: 93-100, 1976.
    • (1976) Eur J Biochem , vol.61 , pp. 93-100
    • Egmond, M.R.1    Brunori, M.2    Fasella, P.M.3
  • 19
    • 0016262599 scopus 로고
    • A multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin
    • Fox JB Jr, Nicholas RA, Ackerman SA, and Swift CE. A multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin. Biochemistry 13: 5178-5186, 1974.
    • (1974) Biochemistry , vol.13 , pp. 5178-5186
    • Fox Jr., J.B.1    Nicholas, R.A.2    Ackerman, S.A.3    Swift, C.E.4
  • 20
    • 0003121376 scopus 로고
    • The presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism
    • Foyer CH and Halliwell B. The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta 133: 21-25, 1976.
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 21
    • 0022411108 scopus 로고
    • Discrepancies among published amino acid sequences of soybean leghemoglobins: Experimental evidence against cultivar differences as the sources of the discrepancies
    • Fuchsman WH. 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.
    • (1985) Arch Biochem Biophys , vol.243 , pp. 454-460
    • Fuchsman, W.H.1
  • 22
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • George P and Irvine DH. The reaction between metmyoglobin and hydrogen peroxide. Biochem J 52: 511-517, 1952.
    • (1952) Biochem J , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 23
    • 0000743530 scopus 로고
    • A possible structure for the higher oxidation state of metmyoglobin
    • George P and Irvine DH. A possible structure for the higher oxidation state of metmyoglobin. Biochem J 60: 596-604, 1955.
    • (1955) Biochem J , vol.60 , pp. 596-604
    • George, P.1    Irvine, D.H.2
  • 24
    • 0000456698 scopus 로고
    • Location of free electrons in porphyrin ring complexes
    • Gibson JF and Ingram DJE. Location of free electrons in porphyrin ring complexes. Nature 178: 871-872, 1956.
    • (1956) Nature , vol.178 , pp. 871-872
    • Gibson, J.F.1    Ingram, D.J.E.2
  • 25
    • 33748392625 scopus 로고
    • Free radical produced in the reaction of metmyoglobin with hydrogen peroxide
    • Gibson JF, Ingram DJE, and Nicholls P. Free radical produced in the reaction of metmyoglobin with hydrogen peroxide. Nature 181: 1398-1399, 1958.
    • (1958) Nature , vol.181 , pp. 1398-1399
    • Gibson, J.F.1    Ingram, D.J.E.2    Nicholls, P.3
  • 26
    • 0027482489 scopus 로고
    • The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects
    • Giulivi C and Cadenas E. The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects. FEBS Lett 332: 287-290, 1993.
    • (1993) FEBS Lett , vol.332 , pp. 287-290
    • Giulivi, C.1    Cadenas, E.2
  • 27
    • 0022396339 scopus 로고
    • Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation
    • Grisham MB. Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation. J Free Radic Biol Med 1: 227-232, 1985.
    • (1985) J Free Radic Biol Med , vol.1 , pp. 227-232
    • Grisham, M.B.1
  • 28
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther MR, Kelman DJ, Corbett JT, and Mason RP. Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J Biol Chem 270: 16075-16081, 1995.
    • (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
  • 29
    • 0034062553 scopus 로고    scopus 로고
    • A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide
    • Gunther MR, Sturgeon BE, and Mason RP. A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Free Radic Biol Med 28: 709-719, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 709-719
    • Gunther, M.R.1    Sturgeon, B.E.2    Mason, R.P.3
  • 30
    • 0022003438 scopus 로고
    • Use of desferrioxamine as a "probe" for iron-dependent formation of hydroxyl radicals. Evidence for a direct reaction between desferal and the superoxide radical
    • Halliwell B. Use of desferrioxamine as a "probe" for iron-dependent formation of hydroxyl radicals. Evidence for a direct reaction between desferal and the superoxide radical. Biochem Pharmacol 34: 229-233, 1985.
    • (1985) Biochem Pharmacol , vol.34 , pp. 229-233
    • Halliwell, B.1
  • 31
    • 0023693165 scopus 로고
    • The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide
    • Harel S and Kanner J. The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide. Free Radic Res Commun 5: 21-33, 1988.
    • (1988) Free Radic Res Commun , vol.5 , pp. 21-33
    • Harel, S.1    Kanner, J.2
  • 33
    • 0034022619 scopus 로고    scopus 로고
    • Pathogenesis of renal failure in rhabdomyolysis: The role of myoglobin
    • Holt S and Moore K. Pathogenesis of renal failure in rhabdomyolysis: the role of myoglobin. Exp Nephrol 8: 72-76, 2000.
    • (2000) Exp Nephrol , vol.8 , pp. 72-76
    • Holt, S.1    Moore, K.2
  • 35
    • 0017505818 scopus 로고
    • E.s.r. studies of peroxy radicals in polyethylene: 1. Temperature dependence of spectra and molecular motion of radical sites
    • Hori Y, Simada S, and Kasiwabara H. E.s.r. studies of peroxy radicals in polyethylene: 1. Temperature dependence of spectra and molecular motion of radical sites. Polymer 18: 567, 1977.
    • (1977) Polymer , vol.18 , pp. 567
    • Hori, Y.1    Simada, S.2    Kasiwabara, H.3
  • 36
    • 0000471154 scopus 로고
    • Change with temperature of the ESR spectra of peroxyl radicals trapped in irradiated polytetrafluoroethylene
    • Iwasaki M and Sakai Y. Change with temperature of the ESR spectra of peroxyl radicals trapped in irradiated polytetrafluoroethylene. J Polym Sci [A-2] 6: 265-279, 1968.
    • (1968) J Polym Sci [A-2] , vol.6 , pp. 265-279
    • Iwasaki, M.1    Sakai, Y.2
  • 37
    • 0032523110 scopus 로고    scopus 로고
    • Comparative radical scavenging ability of bidentate iron (III) chelators
    • Kayyali R, Pannala AS, Khodr H, and Hider RC. Comparative radical scavenging ability of bidentate iron (III) chelators. Biochem Pharmacol 55: 1327-1332, 1998.
    • (1998) Biochem Pharmacol , vol.55 , pp. 1327-1332
    • Kayyali, R.1    Pannala, A.S.2    Khodr, H.3    Hider, R.C.4
  • 38
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen-peroxide forms a peroxyl radical which oxidizes substrates
    • Kelman DJ, DeGray JA, and Mason RP. Reaction of myoglobin with hydrogen-peroxide forms a peroxyl radical which oxidizes substrates. J Biol Chem 269: 7458-7463, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    DeGray, J.A.2    Mason, R.P.3
  • 39
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • Kelso-King NK and Winfield ME. The mechanism of metmyoglobin oxidation. J Biol Chem 238: 1520-1528, 1963.
    • (1963) J Biol Chem , vol.238 , pp. 1520-1528
    • Kelso-King, N.K.1    Winfield, M.E.2
  • 42
    • 0017294736 scopus 로고
    • Renal cortical blood flow in glycerol-induced acute renal failure in the rat
    • Kurtz TW, Maletz RM, and Hsu CH. Renal cortical blood flow in glycerol-induced acute renal failure in the rat. Circ Res 38: 30-35, 1976.
    • (1976) Circ Res , vol.38 , pp. 30-35
    • Kurtz, T.W.1    Maletz, R.M.2    Hsu, C.H.3
  • 43
    • 0027933447 scopus 로고
    • Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage
    • Llesuy SF and Tomaro ML. Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage. Biochim Biophys Acta 1223: 9-14, 1994.
    • (1994) Biochim Biophys Acta , vol.1223 , pp. 9-14
    • Llesuy, S.F.1    Tomaro, M.L.2
  • 44
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in haemoglobin
    • McArthur KM and Davies MJ. Detection and reactions of the globin radical in haemoglobin. Biochim Biophys Acta 1202: 173-181, 1993.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 45
    • 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, Harada K, Yamazaki I, Tamura M, and Watanabe H. 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.
    • (1989) Arch Biochem Biophys , vol.275 , pp. 354-362
    • Miki, H.1    Harada, K.2    Yamazaki, I.3    Tamura, M.4    Watanabe, H.5
  • 46
    • 0030023384 scopus 로고    scopus 로고
    • Hemoglobin induced apolipoprotein B crosslinking in low-density lipoprotein peroxidation
    • Miller YI, Felikman Y, and Shaklai N. Hemoglobin induced apolipoprotein B crosslinking in low-density lipoprotein peroxidation. Arch Biochem Biophys 326: 252-260, 1996.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 252-260
    • Miller, Y.I.1    Felikman, Y.2    Shaklai, N.3
  • 48
    • 0023231486 scopus 로고
    • The enzymatic oxidation of Desferal to a nitroxide free radical
    • Morehouse KM, Flitter WD, and Mason RP. The enzymatic oxidation of Desferal to a nitroxide free radical. FEBS Lett 222: 246-250, 1987.
    • (1987) FEBS Lett , vol.222 , pp. 246-250
    • Morehouse, K.M.1    Flitter, W.D.2    Mason, R.P.3
  • 49
    • 0028838293 scopus 로고
    • Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide
    • Morita T and Kourembanas S. Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide. J Clin Invest 96: 2676-2682, 1995.
    • (1995) J Clin Invest , vol.96 , pp. 2676-2682
    • Morita, T.1    Kourembanas, S.2
  • 50
    • 0025572704 scopus 로고
    • A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism
    • Morrow JD, Hill KE, Burk RF, Nammour TM, Badr KF, and Roberts LJ 2nd. A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism. Proc Natl Acad Sci U S A 87: 9383-9387, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 9383-9387
    • Morrow, J.D.1    Hill, K.E.2    Burk, R.F.3    Nammour, T.M.4    Badr, K.F.5    Roberts II, L.J.6
  • 51
    • 0026443725 scopus 로고
    • Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids
    • Morrow JD, Awad JA, Boss HJ, Blair IA, and Roberts LJ 2nd. Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids. Proc Natl Acad Sci U S A 89: 10721-10725, 1992.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10721-10725
    • Morrow, J.D.1    Awad, J.A.2    Boss, H.J.3    Blair, I.A.4    Roberts II, L.J.5
  • 52
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • Nagababu E and Rifkind JM. Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem Biophys Res Commun 247: 592-596, 1998.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 53
    • 0033847184 scopus 로고    scopus 로고
    • The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo
    • Nath KA, Haggard JJ, Croatt AJ, Grande JP, Poss KD, and Alam J. The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo. Am J Pathol 156: 1527-1535, 2000.
    • (2000) Am J Pathol , vol.156 , pp. 1527-1535
    • Nath, K.A.1    Haggard, J.J.2    Croatt, A.J.3    Grande, J.P.4    Poss, K.D.5    Alam, J.6
  • 54
    • 0035983569 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene therapy for prevention of vasospasm in rats
    • Ono S, Komuro T, and Macdonald RL. Heme oxygenase-1 gene therapy for prevention of vasospasm in rats. J Neurosurg 96: 1094-1102, 2002.
    • (2002) J Neurosurg , vol.96 , pp. 1094-1102
    • Ono, S.1    Komuro, T.2    Macdonald, R.L.3
  • 55
    • 0022273861 scopus 로고
    • Epoxidation of styrene by hemoglobin and myoglobin-transfer of oxidizing equivalents to the protein surface
    • Ortiz de Montellano PR and Catalano CE. Epoxidation of styrene by hemoglobin and myoglobin-transfer of oxidizing equivalents to the protein surface. J Biol Chem 260: 9265-9271, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 9265-9271
    • Ortiz De Montellano, P.R.1    Catalano, C.E.2
  • 56
    • 0025785533 scopus 로고
    • Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase
    • Osawa Y and Korzekwa K. Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase. Proc Natl Acad Sci U S A 88: 7081-7085, 1991.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7081-7085
    • Osawa, Y.1    Korzekwa, K.2
  • 58
    • 0029782103 scopus 로고    scopus 로고
    • Reactions of reactive metabolites with hemoproteins-toxicological implications: Covalent alteration of hemoproteins
    • Osawa Y, Nakatsuka K, Williams MS, Kindt JT, and Nakatsuka M. Reactions of reactive metabolites with hemoproteins-toxicological implications: covalent alteration of hemoproteins. Adv Exp Med Biol 387: 37-45, 1996.
    • (1996) Adv Exp Med Biol , vol.387 , pp. 37-45
    • Osawa, Y.1    Nakatsuka, K.2    Williams, M.S.3    Kindt, J.T.4    Nakatsuka, M.5
  • 59
    • 0032901266 scopus 로고    scopus 로고
    • Carbon monoxide provides protection against hyperoxic lung injury
    • Otterbein LE, Mantell LL, and Choi AM. Carbon monoxide provides protection against hyperoxic lung injury. Am J Physiol 276: L688-L694, 1999.
    • (1999) Am J Physiol , vol.276
    • Otterbein, L.E.1    Mantell, L.L.2    Choi, A.M.3
  • 60
    • 0021329738 scopus 로고
    • Hemoglobin- and hemin-catalyzed transformation of 12L-hydroperoxy-5,8,10, 14-eicosatetraenoic acid
    • Pace-Asciak CR. Hemoglobin- and hemin-catalyzed transformation of 12L-hydroperoxy-5,8,10,14-eicosatetraenoic acid. Biochim Biophys Acta 793: 485-488, 1984.
    • (1984) Biochim Biophys Acta , vol.793 , pp. 485-488
    • Pace-Asciak, C.R.1
  • 62
    • 0002492274 scopus 로고
    • Application of radiation and electron spin resonance spectroscopy to the study of ferryl myoglobin
    • Petersen RL, Symons MCR, and Taiwo FA. Application of radiation and electron spin resonance spectroscopy to the study of ferryl myoglobin. J Chem Soc Faraday Trans I 85: 2435-2443, 1989.
    • (1989) J Chem Soc Faraday Trans I , vol.85 , pp. 2435-2443
    • Petersen, R.L.1    Symons, M.C.R.2    Taiwo, F.A.3
  • 64
    • 0032521652 scopus 로고    scopus 로고
    • Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoicacid
    • Reeder BJ and Wilson MT. Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoicacid. Biochem J 330: 1317-1323, 1998.
    • (1998) Biochem J , vol.330 , pp. 1317-1323
    • Reeder, B.J.1    Wilson, M.T.2
  • 65
    • 0035371323 scopus 로고    scopus 로고
    • The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species
    • Reeder BJ and Wilson MT. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Free Radic Biol Med 30: 1311-1318, 2001.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1311-1318
    • Reeder, B.J.1    Wilson, M.T.2
  • 66
    • 0036670771 scopus 로고    scopus 로고
    • Toxicity of myoglobin and haemoglobin: Oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage
    • Reeder BJ, Sharpe MA, Kay AD, Kerr M, Moore K, and Wilson MT. Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage. Biochem Soc Trans 30: 745-748, 2002.
    • (2002) Biochem Soc Trans , vol.30 , pp. 745-748
    • Reeder, B.J.1    Sharpe, M.A.2    Kay, A.D.3    Kerr, M.4    Moore, K.5    Wilson, M.T.6
  • 67
    • 0037039353 scopus 로고    scopus 로고
    • Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin
    • Reeder BJ, Svistunenko DA, Sharpe MA, and Wilson MT. Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin. Biochemistry 41: 367-375, 2002.
    • (2002) Biochemistry , vol.41 , pp. 367-375
    • Reeder, B.J.1    Svistunenko, D.A.2    Sharpe, M.A.3    Wilson, M.T.4
  • 68
    • 0034652768 scopus 로고    scopus 로고
    • Measurement of F(2)-isoprostanes as an index of oxidative stress in vivo
    • Roberts LJ and Morrow JD. Measurement of F(2)-isoprostanes as an index of oxidative stress in vivo. Free Radic Biol Med 28: 505-513, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 505-513
    • Roberts, L.J.1    Morrow, J.D.2
  • 70
    • 0342618437 scopus 로고    scopus 로고
    • The effects of pH on the oxidation of low-density lipoprotein by copper and metmyoglobin are different
    • Rodriguez-Malaver AJ, Leake DS, and Rice-Evans CA. The effects of pH on the oxidation of low-density lipoprotein by copper and metmyoglobin are different. FEBS Lett 406: 37-41, 1997.
    • (1997) FEBS Lett , vol.406 , pp. 37-41
    • Rodriguez-Malaver, A.J.1    Leake, D.S.2    Rice-Evans, C.A.3
  • 71
    • 0029128032 scopus 로고
    • Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes
    • Rogers MS, Patel RP, Reeder BJ, Sarti P, Wilson MT, and Alayash AI. Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes. Biochem J 310 (Pt 3): 827-833, 1995.
    • (1995) Biochem J , vol.310 , Issue.PART 3 , pp. 827-833
    • Rogers, M.S.1    Patel, R.P.2    Reeder, B.J.3    Sarti, P.4    Wilson, M.T.5    Alayash, A.I.6
  • 72
    • 0036212748 scopus 로고    scopus 로고
    • Nonenzymatic derived lipid peroxide, 8-iso-PGF2 alpha, participates in the pathogenesis of delayed cerebral vasospasm in a canine SAH model
    • Sakamoto M, Takaki E, Yamashita K, Watanabe K, Tabuchi S, Watanabe T, and Satoh K. Nonenzymatic derived lipid peroxide, 8-iso-PGF2 alpha, participates in the pathogenesis of delayed cerebral vasospasm in a canine SAH model. Neurol Res 24: 301-306, 2002.
    • (2002) Neurol Res , vol.24 , pp. 301-306
    • Sakamoto, M.1    Takaki, E.2    Yamashita, K.3    Watanabe, K.4    Tabuchi, S.5    Watanabe, T.6    Satoh, K.7
  • 74
    • 0031027274 scopus 로고    scopus 로고
    • Intracranial aneurysms
    • Schievink WI. Intracranial aneurysms. N Engl J Med 336: 28-40, 1997.
    • (1997) N Engl J Med , vol.336 , pp. 28-40
    • Schievink, W.I.1
  • 75
    • 0000659199 scopus 로고
    • Study of g anisotropy associated with molecular motion in the triphenylmethylperoxy radical. An environmental probe
    • Schlick S and Kevan L. Study of g anisotropy associated with molecular motion in the triphenylmethylperoxy radical. An environmental probe. J Phys Chem 83: 3424-3429, 1979.
    • (1979) J Phys Chem , vol.83 , pp. 3424-3429
    • Schlick, S.1    Kevan, L.2
  • 76
    • 0005404019 scopus 로고
    • Study of lipid peroxyl radicals in urea clathrate crystals. Oxygen-17 coupling and rotational averaging
    • Sevilla MD, Champagne M, and Becker D. Study of lipid peroxyl radicals in urea clathrate crystals. Oxygen-17 coupling and rotational averaging. J Phys Chem 93: 2653-2658, 1989.
    • (1989) J Phys Chem , vol.93 , pp. 2653-2658
    • Sevilla, M.D.1    Champagne, M.2    Becker, D.3
  • 77
    • 0016616098 scopus 로고
    • Electron spin resonance study on peroxidase- and oxidase-reactions of horse radish peroxidase and methemoglobin
    • Shiga T and Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horse radish peroxidase and methemoglobin. Arch Biochem Biophys 167: 469-479, 1975.
    • (1975) Arch Biochem Biophys , vol.167 , pp. 469-479
    • Shiga, T.1    Imaizumi, K.2
  • 79
    • 0031034443 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated alteration of the heme prosthetic group of metmyoglobin to an iron chlorin product: Evidence for a novel oxidative pathway
    • Sugiyama K, Highet RJ, Woods A, Cotter RJ, and Osawa Y. Hydrogen peroxide-mediated alteration of the heme prosthetic group of metmyoglobin to an iron chlorin product: evidence for a novel oxidative pathway. Proc Natl Acad Sci U S A 94: 796-801, 1997.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 796-801
    • Sugiyama, K.1    Highet, R.J.2    Woods, A.3    Cotter, R.J.4    Osawa, Y.5
  • 80
    • 0035820321 scopus 로고    scopus 로고
    • An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins
    • Svistunenko DA. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins. Biochim Biophys Acta 1546: 365-378, 2001.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 365-378
    • Svistunenko, D.A.1
  • 81
    • 0022587766 scopus 로고
    • Paramagnetic centers formed in mouse blood gamma-irradiated at 77K
    • Svistunenko DA, Kosaganova N, and Kopylovskii SA. Paramagnetic centers formed in mouse blood gamma-irradiated at 77K. Radiobiologiia 26: 28-34, 1986.
    • (1986) Radiobiologiia , vol.26 , pp. 28-34
    • Svistunenko, D.A.1    Kosaganova, N.2    Kopylovskii, S.A.3
  • 82
    • 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 DA, Patel RP, and Wilson MT. 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.
    • (1996) Free Radic Res , vol.24 , pp. 269-280
    • Svistunenko, D.A.1    Patel, R.P.2    Wilson, M.T.3
  • 84
    • 0030896551 scopus 로고    scopus 로고
    • The globin-based free radical of ferryl hemoglobin is detected in normal human blood
    • Svistunenko DA, Patel RP, Voloshchenko SV, and Wilson MT. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J Biol Chem 272: 7114-7121, 1997.
    • (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
  • 87
    • 0026667087 scopus 로고
    • Glomerular actions of a free radical-generated novel prostaglandin, 8-epi-prostaglandin F2 alpha, in the rat. Evidence for interaction with thromboxane A2 receptors
    • Takahashi K, Nammour TM, Fukunaga M, Ebert J, Morrow JD, Roberts LJ 2nd, Hoover RL, and Badr KF. Glomerular actions of a free radical-generated novel prostaglandin, 8-epi-prostaglandin F2 alpha, in the rat. Evidence for interaction with thromboxane A2 receptors. J Clin Invest 90: 136-141, 1992.
    • (1992) J Clin Invest , vol.90 , pp. 136-141
    • Takahashi, K.1    Nammour, T.M.2    Fukunaga, M.3    Ebert, J.4    Morrow, J.D.5    Roberts II, L.J.6    Hoover, R.L.7    Badr, K.F.8
  • 88
    • 0025744459 scopus 로고
    • The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs
    • Turner JJ, Rice-Evans CA, Davies MJ, and Newman ES. The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs. Biochem J 277: 833-837, 1991.
    • (1991) Biochem J , vol.277 , pp. 833-837
    • Turner, J.J.1    Rice-Evans, C.A.2    Davies, M.J.3    Newman, E.S.4
  • 89
    • 0017225682 scopus 로고
    • The vascular basis for acute renal failure in the rat. Preglomerular and postglomerular vasoconstriction
    • Venkatachalam MA, Rennke HG, and Sandstrom DJ. The vascular basis for acute renal failure in the rat. Preglomerular and postglomerular vasoconstriction. Circ Res 38: 267-279, 1976.
    • (1976) Circ Res , vol.38 , pp. 267-279
    • Venkatachalam, M.A.1    Rennke, H.G.2    Sandstrom, D.J.3
  • 91
    • 0034708352 scopus 로고    scopus 로고
    • Enhanced lipid oxidation by oxidatively modified myoglobin: Role of protein-bound heme
    • Vuletich JL, Osawa Y, and Aviram M. Enhanced lipid oxidation by oxidatively modified myoglobin: role of protein-bound heme. Biochem Biophys Res Commun 269: 647-651, 2000.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 647-651
    • Vuletich, J.L.1    Osawa, Y.2    Aviram, M.3
  • 92
    • 0021041598 scopus 로고
    • Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid
    • Walters FP, Kennedy FG, and Jones DP. Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid. FEBS Lett 163: 292-296, 1983.
    • (1983) FEBS Lett , vol.163 , pp. 292-296
    • Walters, F.P.1    Kennedy, F.G.2    Jones, D.P.3
  • 93
    • 0032815398 scopus 로고    scopus 로고
    • Characterization of acute reversible systemic hypertension in a model of heme protein-induced renal injury
    • Warden DH, Croatt AJ, Katusic ZS, and Nath KA. Characterization of acute reversible systemic hypertension in a model of heme protein-induced renal injury. Am J Physiol 277: F58-F65, 1999.
    • (1999) Am J Physiol , vol.277
    • Warden, D.H.1    Croatt, A.J.2    Katusic, Z.S.3    Nath, K.A.4
  • 94
    • 0027179846 scopus 로고
    • Polyunsaturated fatty acid alkoxyl radicals exist as carbon-centered epoxyallylic radicals: A key step in hydroperoxide-amplified lipid peroxidation
    • Wilcox AL and Marnett LJ. Polyunsaturated fatty acid alkoxyl radicals exist as carbon-centered epoxyallylic radicals: a key step in hydroperoxide-amplified lipid peroxidation. Chem Res Toxicol 6: 413-416, 1993.
    • (1993) Chem Res Toxicol , vol.6 , pp. 413-416
    • Wilcox, A.L.1    Marnett, L.J.2
  • 96
    • 0014216604 scopus 로고
    • Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase
    • Yonetani T and Schleyer H. Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase. J Biol Chem 242: 1974-1979, 1967.
    • (1967) J Biol Chem , vol.242 , pp. 1974-1979
    • Yonetani, T.1    Schleyer, H.2
  • 97
    • 0024405028 scopus 로고
    • Studies of mechanisms and protective maneuvers in myoglobinuric acute renal injury
    • Zager RA. Studies of mechanisms and protective maneuvers in myoglobinuric acute renal injury. Lab Invest 60: 619-629, 1989.
    • (1989) Lab Invest , vol.60 , pp. 619-629
    • Zager, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.