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Volumn 2, Issue 1, 1998, Pages 37-44

Effect of nitric oxide on hemoprotein-catalyzed oxidative reactions

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN; NITRIC OXIDE;

EID: 0032004514     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1006/niox.1998.0167     Document Type: Article
Times cited : (56)

References (37)
  • 1
  • 2
    • 0023900998 scopus 로고
    • Neutrophil-mediated mucosal injury. Role of reactive oxygen metabolites
    • Grisham M. B., Granger D. N. Neutrophil-mediated mucosal injury. Role of reactive oxygen metabolites. Dig. Dis. Sci. 33:1988;6S-15S.
    • (1988) Dig. Dis. Sci. , vol.33
    • Grisham, M.B.1    Granger, D.N.2
  • 3
    • 0022918956 scopus 로고
    • The role of antioxidants in the retina and retinal pigment epithelium and the nature of prooxidant-induced damage
    • Handelman G. J., Dratz E. A. The role of antioxidants in the retina and retinal pigment epithelium and the nature of prooxidant-induced damage. Adv. Free Radical Biol. Med. 2:1986;1-89.
    • (1986) Adv. Free Radical Biol. Med. , vol.2 , pp. 1-89
    • Handelman, G.J.1    Dratz, E.A.2
  • 4
    • 0021879738 scopus 로고
    • Effect of blood on the activity and persistence of antigen-induced inflammation in the rat air pouch
    • Yoshino S., Blake D. R., Hewitt S., Morris C., Bacon P. A. Effect of blood on the activity and persistence of antigen-induced inflammation in the rat air pouch. Ann. Rheum. Dis. 44:1985;485-490.
    • (1985) Ann. Rheum. Dis. , vol.44 , pp. 485-490
    • Yoshino, S.1    Blake, D.R.2    Hewitt, S.3    Morris, C.4    Bacon, P.A.5
  • 5
    • 0023755521 scopus 로고
    • Hemoglobin and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity
    • Paller M. S. Hemoglobin and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity. Am. J. Physiol. 255:1988;F539-F544.
    • (1988) Am. J. Physiol. , vol.255
    • Paller, M.S.1
  • 6
    • 0021288367 scopus 로고
    • 2-induced lipid peroxidation and focal edema in rat brain
    • 2-induced lipid peroxidation and focal edema in rat brain. Exp. Neurol. 83:1984;62.
    • (1984) Exp. Neurol. , vol.83 , pp. 62
    • Willmore, L.J.1    Rubin, J.J.2
  • 8
    • 0024242512 scopus 로고
    • Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate
    • Sadrzadeh S. M. H., Eaton J. W. Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate. J. Clin. Invest. 82:1988;1510.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1510
    • Sadrzadeh, S.M.H.1    Eaton, J.W.2
  • 9
    • 0014747971 scopus 로고
    • Evaluation of renal toxicity of hemoproteins and their derivatives: A role in the genesis of acute tubule necrosis
    • Braun S. R., Weiss F. R., Keller A. L., Ciccone J. R., Preuss H. G. Evaluation of renal toxicity of hemoproteins and their derivatives: A role in the genesis of acute tubule necrosis. J. Exp. Med. 131:1970;443.
    • (1970) J. Exp. Med. , vol.131 , pp. 443
    • Braun, S.R.1    Weiss, F.R.2    Keller, A.L.3    Ciccone, J.R.4    Preuss, H.G.5
  • 10
    • 0019957619 scopus 로고
    • Possible role for cytotoxic oxygen metabolites in the pathogenesis of cardiac ischemic reperfusion
    • Shlafer M., Kane P. F., Wiggens V. Y., Kirsh M. M. Possible role for cytotoxic oxygen metabolites in the pathogenesis of cardiac ischemic reperfusion. Circulation. 66:1982;1-85.
    • (1982) Circulation , vol.66 , pp. 1-85
    • Shlafer, M.1    Kane, P.F.2    Wiggens, V.Y.3    Kirsh, M.M.4
  • 11
    • 0021343227 scopus 로고
    • Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase
    • Jolly S. R., Kane W. J., Bartie M. B., Abrams G. D., Lucchesi B. R. Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase. Circ. Res. 54:1984;277.
    • (1984) Circ. Res. , vol.54 , pp. 277
    • Jolly, S.R.1    Kane, W.J.2    Bartie, M.B.3    Abrams, G.D.4    Lucchesi, B.R.5
  • 12
    • 0022411604 scopus 로고
    • Enhancement of recovery of myocardial function by oxygen free radical scavengers after reversible ischemia
    • Myers M. L., Bolli R., Lekich R. F., Hartley C. J., Robers R. Enhancement of recovery of myocardial function by oxygen free radical scavengers after reversible ischemia. Circulation. 72:1985;915.
    • (1985) Circulation , vol.72 , pp. 915
    • Myers, M.L.1    Bolli, R.2    Lekich, R.F.3    Hartley, C.J.4    Robers, R.5
  • 13
    • 0022639077 scopus 로고
    • Superoxide dismutase plus catalase improve contractile formation in the canine model of the stunned myocardium
    • Przyklenk K., Kloner R. A. Superoxide dismutase plus catalase improve contractile formation in the canine model of the stunned myocardium. Circ. Res. 58:1986;148.
    • (1986) Circ. Res. , vol.58 , pp. 148
    • Przyklenk, K.1    Kloner, R.A.2
  • 15
    • 0022555420 scopus 로고
    • Leukocytes and ischemia-induced myocardial injury
    • Lucchesi B. R. Leukocytes and ischemia-induced myocardial injury. Annu. Rev. Pharmacol. Toxicol. 26:1986;201.
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 201
    • Lucchesi, B.R.1
  • 16
    • 0001608604 scopus 로고
    • Peroxidant activity of hemoglobin and myoglobin
    • Boston: CRC Press. p. 335-344
    • Grisham M. B. Peroxidant activity of hemoglobin and myoglobin. Peroxidases in Chemistry and Biology. 1991;CRC Press, Boston. p. 335-344.
    • (1991) Peroxidases in Chemistry and Biology
    • Grisham, M.B.1
  • 17
    • 0019202643 scopus 로고
    • Nitric oxide myoglobin as an inhibitor of lipid peroxidation
    • Kanner J., Ben-Gera I., Berman S. Nitric oxide myoglobin as an inhibitor of lipid peroxidation. Lipids. 15:1979;944-948.
    • (1979) Lipids , vol.15 , pp. 944-948
    • Kanner, J.1    Ben-Gera, I.2    Berman, S.3
  • 19
    • 0029815841 scopus 로고    scopus 로고
    • Nitric oxide and metal-catalyzed reactions
    • Kanner J. Nitric oxide and metal-catalyzed reactions. Methods Enzymol. 269:1996;218-229.
    • (1996) Methods Enzymol. , vol.269 , pp. 218-229
    • Kanner, J.1
  • 20
    • 0029069277 scopus 로고
    • Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: A protective mechanism against ferryl hemoprotein-induced oxidations
    • Gorbunov N. V., Osipov A. N., Day B. W., Zayas-Rivera B., Kagan V. E., Elsayed N. M. Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: A protective mechanism against ferryl hemoprotein-induced oxidations. Biochemistry. 34:1995;6689-6699.
    • (1995) Biochemistry , vol.34 , pp. 6689-6699
    • Gorbunov, N.V.1    Osipov, A.N.2    Day, B.W.3    Zayas-Rivera, B.4    Kagan, V.E.5    Elsayed, N.M.6
  • 23
    • 0026002394 scopus 로고
    • The modulation of ferryl myoglobin formation and its antioxidative effects on low density lipoproteins by nitric oxide
    • Dee G., Rice-Evans C., Obeyesekera S., Meraji S., Jacobs M., Bruckdorfer K. R. The modulation of ferryl myoglobin formation and its antioxidative effects on low density lipoproteins by nitric oxide. FEBS Lett. 294:1991;38-42.
    • (1991) FEBS Lett. , vol.294 , pp. 38-42
    • Dee, G.1    Rice-Evans, C.2    Obeyesekera, S.3    Meraji, S.4    Jacobs, M.5    Bruckdorfer, K.R.6
  • 25
    • 0021160336 scopus 로고
    • A quantitative fluorometric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorometric assay of cellular activation processes
    • Hyslop P. A., Sklar L. A. A quantitative fluorometric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorometric assay of cellular activation processes. Anal. Biochem. 141:1984;280-286.
    • (1984) Anal. Biochem. , vol.141 , pp. 280-286
    • Hyslop, P.A.1    Sklar, L.A.2
  • 28
    • 0028116941 scopus 로고
    • Total antioxidant status in plasma and body fluids
    • Rice-Evans C., Miller N. Total antioxidant status in plasma and body fluids. Methods Enzymol. 234:1994;279-293.
    • (1994) Methods Enzymol. , vol.234 , pp. 279-293
    • Rice-Evans, C.1    Miller, N.2
  • 29
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • Kelso King N., Winfield M. E. The mechanism of metmyoglobin oxidation. J. Biol. Chem. 238:1963;1520-1528.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • Kelso King, N.1    Winfield, M.E.2
  • 30
    • 0000322203 scopus 로고
    • Oxidation and reduction of hemoproteins by trioxodinitrate(II). The role of nytrosyl hydride and nitrite
    • Doyle M. P., Mahapatro S. N., Broene R. D., Guy J. K. Oxidation and reduction of hemoproteins by trioxodinitrate(II). The role of nytrosyl hydride and nitrite. J. Am. Chem. Soc. 110:1988;593-599.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 593-599
    • Doyle, M.P.1    Mahapatro, S.N.2    Broene, R.D.3    Guy, J.K.4
  • 31
    • 0024595597 scopus 로고
    • Oxidation of dimethylsulfoxide to formaldehyde by oxyhaemoglobin and oxyleghaemoglobin in the presence of hydrogen peroxide is not mediated by "free" hydroxyl radicals
    • Puppo A., Halliwell B. Oxidation of dimethylsulfoxide to formaldehyde by oxyhaemoglobin and oxyleghaemoglobin in the presence of hydrogen peroxide is not mediated by "free" hydroxyl radicals. Free Radicals Res. Commun. 5:1989;277-281.
    • (1989) Free Radicals Res. Commun. , vol.5 , pp. 277-281
    • Puppo, A.1    Halliwell, B.2
  • 33
    • 0000399717 scopus 로고
    • Photochemistry of nitric oxide adducts of water-solubleiron(III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysis
    • Hoshino M., Ozawa K., Seki H., Ford P. C. Photochemistry of nitric oxide adducts of water-solubleiron(III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysis. J. Am. Chem. Soc. 115:1993;9568-9575.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9568-9575
    • Hoshino, M.1    Ozawa, K.2    Seki, H.3    Ford, P.C.4
  • 34
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxides by bound dioxygen in hemoproteins
    • Doyle M. P., Hoekstra J. W. Oxidation of nitrogen oxides by bound dioxygen in hemoproteins. J. Inorg. Biochem. 14:1981;351-358.
    • (1981) J. Inorg. Biochem. , vol.14 , pp. 351-358
    • Doyle, M.P.1    Hoekstra, J.W.2
  • 35
    • 0014216132 scopus 로고
    • Studies on the equilibria and kinetics of the reactions of peroxidase with ligands
    • Wittenberg J. B., Noble R. W., Wittenberg B. A., Brunori E. A., Wyman J. Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. J. Biol. Chem. 242:1967;626-634.
    • (1967) J. Biol. Chem. , vol.242 , pp. 626-634
    • Wittenberg, J.B.1    Noble, R.W.2    Wittenberg, B.A.3    Brunori, E.A.4    Wyman, J.5
  • 36
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxinitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman J. S., Beckman T. W., Chen J., Marshall P. A., Freeman B. A. Apparent hydroxyl radical production by peroxinitrite: Implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA. 87:1990;1620-1624.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.