메뉴 건너뛰기




Volumn 30, Issue 11, 2001, Pages 1311-1318

The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species

Author keywords

Ferric ferryl; Free radicals; Haemin; HPODE; Myoglobin; Peroxides; pH; Rhabdomyolysis

Indexed keywords

FERRYLMYOGLOBIN; HEMIN; HYDROGEN PEROXIDE; LIPID HYDROPEROXIDE; LIPID PEROXIDASE;

EID: 0035371323     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(01)00534-2     Document Type: Article
Times cited : (100)

References (35)
  • 1
    • 0024324796 scopus 로고
    • Mechanisms of reoxygenation injury in myocardial infarction: Implications of a myoglobin redox cycle
    • Galaris D., Eddy L., Arduini A., Cadenas E., Hochstein P. Mechanisms of reoxygenation injury in myocardial infarction implications of a myoglobin redox cycle . Biochem. Biophys. Res. Commun. 160:1989;1162-1168.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1162-1168
    • Galaris, D.1    Eddy, L.2    Arduini, A.3    Cadenas, E.4    Hochstein, P.5
  • 2
    • 0024444665 scopus 로고
    • Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle
    • Galaris D., Cadenas E., Hochstein P. Redox cycling of myoglobin and ascorbate a potential protective mechanism against oxidative reperfusion injury in muscle . Arch. Biochem. Biophys. 273:1989;497-504.
    • (1989) Arch. Biochem. Biophys. , vol.273 , pp. 497-504
    • Galaris, D.1    Cadenas, E.2    Hochstein, P.3
  • 3
    • 0033045583 scopus 로고    scopus 로고
    • Potential roles of myoglobin autoxidation in myocardial ischemia-reperfusion injury
    • Gunther M.R., Sampath V., Caughey W.S. Potential roles of myoglobin autoxidation in myocardial ischemia-reperfusion injury. Free Radic. Biol. Med. 26:1999;1388-1395.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 1388-1395
    • Gunther, M.R.1    Sampath, V.2    Caughey, W.S.3
  • 4
    • 0033969034 scopus 로고    scopus 로고
    • Effects of hypoxia and glutathione depletion on hemoglobin- And myoglobin-mediated oxidative stress toward endothelium
    • D'Agnillo F., Wood F., Porras C., Macdonald V.W., Alayash A.I. Effects of hypoxia and glutathione depletion on hemoglobin- and myoglobin-mediated oxidative stress toward endothelium. Biochim. Biophys. Acta. 1495:2000;150-159.
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 150-159
    • D'Agnillo, F.1    Wood, F.2    Porras, C.3    Macdonald, V.W.4    Alayash, A.I.5
  • 9
    • 0028267350 scopus 로고
    • Reactivity of metmyoglobin towards phospholipid hydroperoxides
    • Maiorino M., Ursini F., Cadenas E. Reactivity of metmyoglobin towards phospholipid hydroperoxides. Free Radic. Biol. Med. 16:1994;661-667.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 661-667
    • Maiorino, M.1    Ursini, F.2    Cadenas, E.3
  • 11
    • 0029128032 scopus 로고
    • Pro-oxidant effects of cross-linked haemoglobin explored using liposome and cytochrome c oxidase vesicle model membranes
    • Rogers M.S., Patel R.P., Reeder B.J., Sarti P., Wilson M.T., Alayash A.I. Pro-oxidant effects of cross-linked haemoglobin explored using liposome and cytochrome c oxidase vesicle model membranes. Biochem. J. 310:1995;827-833.
    • (1995) Biochem. J. , vol.310 , 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
  • 12
    • 0342618437 scopus 로고    scopus 로고
    • The effects of pH on the oxidation of low-density lipoprotein by copper and metmyoglobin are different
    • Rodriguez-Malaver A.J., Leake D.S., Rice-Evans C.A. The effects of pH on the oxidation of low-density lipoprotein by copper and metmyoglobin are different. FEBS Lett. 406:1997;37-41.
    • (1997) FEBS Lett. , vol.406 , pp. 37-41
    • Rodriguez-Malaver, A.J.1    Leake, D.S.2    Rice-Evans, C.A.3
  • 13
    • 0026532276 scopus 로고
    • The interaction between ruptured erythrocytes and low-density lipoproteins
    • Paganga G., Rice-Evans C.A., Rule R., Leake D. The interaction between ruptured erythrocytes and low-density lipoproteins. FEBS Lett. 303:1992;154-158.
    • (1992) FEBS Lett. , vol.303 , pp. 154-158
    • Paganga, G.1    Rice-Evans, C.A.2    Rule, R.3    Leake, D.4
  • 14
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • King N.K., Winfield M.E. 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
  • 16
    • 0025616146 scopus 로고
    • Detection of ferryl myoglobin in the isolated ischemic rat-heart
    • Arduini A., Eddy L., Hochstein P. Detection of ferryl myoglobin in the isolated ischemic rat-heart. Free Radic. Biol. Med. 9:1990;511-513.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 511-513
    • Arduini, A.1    Eddy, L.2    Hochstein, P.3
  • 17
    • 0026045865 scopus 로고
    • Identification of initiating agents in myoglobin-induced lipid peroxidation
    • Newman E.S.R., Rice-Evans C.A., Davies M.J. Identification of initiating agents in myoglobin-induced lipid peroxidation. Biochem. Biophys. Res. Commun. 179:1991;1414-1419.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1414-1419
    • Newman, E.S.R.1    Rice-Evans, C.A.2    Davies, M.J.3
  • 18
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in hemoglobin
    • McArther K.M., Davies M.J. Detection and reactions of the globin radical in hemoglobin. Biochim. Biophys. Acta. 1202:1993;173-181.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 173-181
    • McArther, K.M.1    Davies, M.J.2
  • 19
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • George P., Irvine D.H. 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
  • 20
    • 0007842933 scopus 로고
    • The reaction between metmyoglobin and alkyl hydroperoxes
    • George P., Irvine D.H. The reaction between metmyoglobin and alkyl hydroperoxes. Biochem. J. 55:1953;230-236.
    • (1953) Biochem. J. , vol.55 , pp. 230-236
    • George, P.1    Irvine, D.H.2
  • 21
    • 0032521652 scopus 로고    scopus 로고
    • Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid
    • Reeder B.J., Wilson M.T. Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid. Biochem. J. 330:1998;1317-1323.
    • (1998) Biochem. J. , vol.330 , pp. 1317-1323
    • Reeder, B.J.1    Wilson, M.T.2
  • 22
    • 0342467554 scopus 로고
    • Reaction between lipid hydroperoxide and hemoglobin studied by a spectrophotometric and a spin trapping method
    • Aoshima H., Yoshida Y., Taniguichi H. Reaction between lipid hydroperoxide and hemoglobin studied by a spectrophotometric and a spin trapping method. Agric. Biol. Chem. 50:1986;1777-1783.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 1777-1783
    • Aoshima, H.1    Yoshida, Y.2    Taniguichi, H.3
  • 23
    • 0021329738 scopus 로고
    • L-hydroperoxy-5,8,10,14-eicosatetraenoic acid
    • L-hydroperoxy-5,8,10,14-eicosatetraenoic acid. Biochim. Biophys. Acta. 793:1984;485-488.
    • (1984) Biochim. Biophys. Acta , vol.793 , pp. 485-488
    • Pace-Asciak, C.R.1
  • 24
    • 0027179846 scopus 로고
    • Polyunsaturated fatty-acid alkoxyl radicals exist as carbon-centered epoxyallylic radicals - A key step in hydroperoxide-amplified lipid-peroxidation
    • Wilcox A.L., Marnett L.J. Polyunsaturated fatty-acid alkoxyl radicals exist as carbon-centered epoxyallylic radicals - a key step in hydroperoxide-amplified lipid-peroxidation. Chem. Res. Toxicol. 6:1993;413-416.
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 413-416
    • Wilcox, A.L.1    Marnett, L.J.2
  • 25
    • 0003796319 scopus 로고
    • A. Neuberger, & E.L. Tatum. Amsterdam, London: North-Holland Publishing Company
    • Antonini E., Brunori M. Neuberger A., Tatum E.L. Frontiers in biology. 1971;1-52 North-Holland Publishing Company, Amsterdam, London.
    • (1971) Frontiers in Biology , pp. 1-52
    • Antonini, E.1    Brunori, M.2
  • 27
    • 0021842958 scopus 로고
    • Conversion of linoleic-acid hydroperoxide to hydroxy, keto, epoxyhydroxy, and trihydroxy fatty-acids by hematin
    • Dix T.A., Marnett L.J. Conversion of linoleic-acid hydroperoxide to hydroxy, keto, epoxyhydroxy, and trihydroxy fatty-acids by hematin. J. Biol. Chem. 260:1985;5351-5371.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5351-5371
    • Dix, T.A.1    Marnett, L.J.2
  • 28
    • 0021864205 scopus 로고
    • Hematin-catalyzed epoxidation of 7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene by poly-unsaturated fatty-acid hydroperoxides
    • Dix T.A., Fontana R., Pantham A., Marnett L.J. Hematin-catalyzed epoxidation of 7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene by poly-unsaturated fatty-acid hydroperoxides. J. Biol. Chem. 260:1985;5338-5365.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5338-5365
    • Dix, T.A.1    Fontana, R.2    Pantham, A.3    Marnett, L.J.4
  • 29
    • 33751269828 scopus 로고
    • Dynamics of (meso-tetrakis(2,6-dimethyl-3-sulfonatophenyl)porphinato)-iron(III) hydrate with tert-butyl hydroperoxide in aqueous solution. 2. Establishment of a mechanism that involves homolytic O-O bond breaking and one-electron oxidation of the iron (III) porphyrin
    • Balasubramanian P.N., Smith J.R.L., Davies M.J., Kaaret T.W., Bruice T.C. Dynamics of (meso-tetrakis(2,6-dimethyl-3-sulfonatophenyl)porphinato)-iron(III) hydrate with tert-butyl hydroperoxide in aqueous solution. 2. Establishment of a mechanism that involves homolytic O-O bond breaking and one-electron oxidation of the iron (III) porphyrin. J. Am. Chem. Soc. 111:1989;1477-1483.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1477-1483
    • Balasubramanian, P.N.1    Smith, J.R.L.2    Davies, M.J.3    Kaaret, T.W.4    Bruice, T.C.5
  • 30
    • 0015239532 scopus 로고
    • Sulfheme proteins: Optical and magnetic properties of sulfmyoglobin and its derivatives
    • Berzofsky J.A., Peisach J., Blumberg W.E. Sulfheme proteins optical and magnetic properties of sulfmyoglobin and its derivatives . J. Biol. Chem. 246:1971;3367-3377.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3367-3377
    • Berzofsky, J.A.1    Peisach, J.2    Blumberg, W.E.3
  • 31
    • 0021041598 scopus 로고
    • Oxidation of myoglobin in isolated adult-rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid
    • Walters F.P., Kennedy F.G., Jones D.P. Oxidation of myoglobin in isolated adult-rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid. FEBS Lett. 163:1983;292-296.
    • (1983) FEBS Lett. , vol.163 , pp. 292-296
    • Walters, F.P.1    Kennedy, F.G.2    Jones, D.P.3
  • 32
    • 0025785533 scopus 로고
    • Oxidative modification by low-levels of HOOH can transform myoglobin to an oxidase
    • Osawa Y., Korzekwa K. Oxidative modification by low-levels of HOOH can transform myoglobin to an oxidase. Proc. Natl. Acad. Sci. USA. 88:1991;7081-7085.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7081-7085
    • Osawa, Y.1    Korzekwa, K.2
  • 33
    • 0031389884 scopus 로고    scopus 로고
    • Vitamin E may slow kidney failure owing to oxidative stress
    • Fryer M.J. Vitamin E may slow kidney failure owing to oxidative stress. Redox Rep. 3:1997;259-261.
    • (1997) Redox Rep. , vol.3 , pp. 259-261
    • Fryer, M.J.1
  • 34
    • 0025744459 scopus 로고
    • The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs
    • Turner J., Rice-Evans C., Davies M., Newman E. The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs. Biochem. J. 227:1991;833-837.
    • (1991) Biochem. J. , vol.227 , pp. 833-837
    • Turner, J.1    Rice-Evans, C.2    Davies, M.3    Newman, E.4
  • 35
    • 0023231486 scopus 로고
    • The enzymatic oxidation of desferal to a nitroxide free-radical
    • Morehouse K., Flitter W., Mason R. The enzymatic oxidation of desferal to a nitroxide free-radical. FEBS Lett. 222:1987;246-250.
    • (1987) FEBS Lett. , vol.222 , pp. 246-250
    • Morehouse, K.1    Flitter, W.2    Mason, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.