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Volumn 9, Issue 8, 1996, Pages 1382-1390

Reactions of oxymyoglobin with NO, NO2, and NO2- under argon and in air

Author keywords

[No Author keywords available]

Indexed keywords

ARGON; GUANYLATE CYCLASE; METMYOGLOBIN; MYOGLOBIN; NITROGEN DIOXIDE; NITROUS OXIDE; OXYHEMOGLOBIN; OZONE; PORPHYRIN; NITRATE; OXYMYOGLOBIN; PEROXYNITRIC ACID;

EID: 0029658154     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx9600457     Document Type: Article
Times cited : (64)

References (46)
  • 1
    • 0344478773 scopus 로고
    • The reactions of nitrite with hemoglobin derivatives
    • Barnard, R. D. (1937) The reactions of nitrite with hemoglobin derivatives. J. Biol. Chem. 120, 177-191.
    • (1937) J. Biol. Chem. , vol.120 , pp. 177-191
    • Barnard, R.D.1
  • 2
    • 0022313068 scopus 로고
    • Autocatalytic oxidation of hemoglobin induced by nitrite. Activation and chemical inhibition
    • Doyle, M. P., Herman, J. G., and Dykstra, R. L. (1988) Autocatalytic oxidation of hemoglobin induced by nitrite. Activation and chemical inhibition. J. Free Radicals Biol. Med. 1, 145-153.
    • (1988) J. Free Radicals Biol. Med. , vol.1 , pp. 145-153
    • Doyle, M.P.1    Herman, J.G.2    Dykstra, R.L.3
  • 3
    • 0020918418 scopus 로고
    • The reaction between hemoglobin and nitrite
    • Jung, F., and Spolaczyk, M. (1983) The reaction between hemoglobin and nitrite. Biomed. Biochem. Acta 42 (22-12 Suppl.), 149-153.
    • (1983) Biomed. Biochem. Acta , vol.42 , Issue.12-22 SUPPL. , pp. 149-153
    • Jung, F.1    Spolaczyk, M.2
  • 4
    • 0020951461 scopus 로고
    • Detection of paramagnetic species in the autocatalytic reaction between nitrite and hemoglobin
    • Ebert, B., Lassaman, G., and Jung, F. (1983) Detection of paramagnetic species in the autocatalytic reaction between nitrite and hemoglobin. Biomed. Biochem. Acta 42, 154.
    • (1983) Biomed. Biochem. Acta , vol.42 , pp. 154
    • Ebert, B.1    Lassaman, G.2    Jung, F.3
  • 5
    • 0024990402 scopus 로고
    • Formation of methemoglobin and metmyoglobin using 8-amino-quinoline derivatives or sodium nitrite and subsequent reaction with cyanide
    • Steinhaus, R. K., Baskin, S. I., Clark, J. H., and Kirby, S. D. (1990) Formation of methemoglobin and metmyoglobin using 8-amino-quinoline derivatives or sodium nitrite and subsequent reaction with cyanide. J. Appl. Toxicol. 10, 345-351.
    • (1990) J. Appl. Toxicol. , vol.10 , pp. 345-351
    • Steinhaus, R.K.1    Baskin, S.I.2    Clark, J.H.3    Kirby, S.D.4
  • 6
    • 0016429979 scopus 로고
    • Mechanism for the autoxidation of hemoglobin by phenols, nitrite, and oxidant drugs. Peroxide formation by one electron donation to bound dioxygen
    • Wallace, W. J., and Caughey, W. S. (1975) Mechanism for the autoxidation of hemoglobin by phenols, nitrite, and oxidant drugs. Peroxide formation by one electron donation to bound dioxygen. Biochem. Biophys. Res. Commun. 62, 561-567.
    • (1975) Biochem. Biophys. Res. Commun. , vol.62 , pp. 561-567
    • Wallace, W.J.1    Caughey, W.S.2
  • 7
    • 0022514569 scopus 로고
    • The kinetic differences between sodium nitrite, amyl nitrite, and nitroglycerine oxidation of hemoglobin
    • Tarburton, J. P., and Metcalf, W. Y. (1986) The kinetic differences between sodium nitrite, amyl nitrite, and nitroglycerine oxidation of hemoglobin. Histol. Histopath. 1, 213-217.
    • (1986) Histol. Histopath. , vol.1 , pp. 213-217
    • Tarburton, J.P.1    Metcalf, W.Y.2
  • 8
    • 49849113152 scopus 로고
    • Nitrates, nitrites, methemoglobinemia
    • Lee, D. H. K. (1970) Nitrates, nitrites, methemoglobinemia. Environ. Res. 3, 481-511.
    • (1970) Environ. Res. , vol.3 , pp. 481-511
    • Lee, D.H.K.1
  • 9
    • 0008453394 scopus 로고
    • Mammalian Syntheses of Nitrite, Nitrate, and Nitric Oxide and Nitrosating Agents
    • (Marnett, L. J., Ed.) Chapter 6, American Chemical Society, Washington, DC
    • Marletta, M. A. (1992) Mammalian Syntheses of Nitrite, Nitrate, and Nitric Oxide and Nitrosating Agents. In Frontiers Molecular Toxicology (Marnett, L. J., Ed.) Chapter 6, pp 46-54, American Chemical Society, Washington, DC.
    • (1992) Frontiers Molecular Toxicology , pp. 46-54
    • Marletta, M.A.1
  • 10
    • 0027326619 scopus 로고
    • The biological role of nitric oxide in bacteria
    • Zumft, W. G. (1993) The biological role of nitric oxide in bacteria. Arch. Microbiol. 253-264.
    • (1993) Arch. Microbiol. , pp. 253-264
    • Zumft, W.G.1
  • 11
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxide by bound dioxygen in heme proteins
    • Doyle, N. P., and Hoekstra, J. W. (1981) Oxidation of nitrogen oxide by bound dioxygen in heme proteins. J. Inorg. Biochem. 14, 351-358.
    • (1981) J. Inorg. Biochem. , vol.14 , pp. 351-358
    • Doyle, N.P.1    Hoekstra, J.W.2
  • 12
    • 0001637417 scopus 로고
    • Spectrophotometric determination of nitric oxide using hemoglobin
    • Nowack, E., Kubitzek, D., and Kojda, G. (1992) Spectrophotometric determination of nitric oxide using hemoglobin. Neuro Procotcols 1, 133-139.
    • (1992) Neuro Procotcols , vol.1 , pp. 133-139
    • Nowack, E.1    Kubitzek, D.2    Kojda, G.3
  • 13
    • 0027447237 scopus 로고
    • Measurement of nitric oxide in biological models
    • Archer, S. (1993) Measurement of nitric oxide in biological models. FASEB J. 7, 349-368.
    • (1993) FASEB J. , vol.7 , pp. 349-368
    • Archer, S.1
  • 14
    • 0027276333 scopus 로고
    • Nitric oxide and cardiovascular control
    • Calver, A., Collier, J., and Valance, P. (1993) Nitric oxide and cardiovascular control. Expl. Physiol. 78, 303-326.
    • (1993) Expl. Physiol. , vol.78 , pp. 303-326
    • Calver, A.1    Collier, J.2    Valance, P.3
  • 15
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. (1992) Nitric oxide as a secretory product of mammalian cells. FASEB J. 6, 3051-3064.
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 16
    • 0000709856 scopus 로고
    • Chemistry relevant to the biological effects of nitric oxide and metallonitrosyls
    • (Clarke, M. J., Goodenough, J. B., Ibers, J. A., Jørgensen, C. K., Mingos, D. M. P., Nielands, J. B., Palmer, G. A., Reinen, D., Sadler, P. J., Weiss, R., and Williams, R. J. P., Eds.) Springer-Verlag, Berlin
    • Clarke, M. J., and Gaul, J. (1993) Chemistry relevant to the biological effects of nitric oxide and metallonitrosyls. In Structure and Bonding (Clarke, M. J., Goodenough, J. B., Ibers, J. A., Jørgensen, C. K., Mingos, D. M. P., Nielands, J. B., Palmer, G. A., Reinen, D., Sadler, P. J., Weiss, R., and Williams, R. J. P., Eds.) pp 147-181, Springer-Verlag, Berlin.
    • (1993) Structure and Bonding , pp. 147-181
    • Clarke, M.J.1    Gaul, J.2
  • 17
    • 0025883342 scopus 로고
    • Nitrict oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R. M. J., and Higgs, E. A. (1991) Nitrict oxide: Physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 19
    • 0001373384 scopus 로고
    • Kinetics of N-nitrosation in oxygenated nitric oxide solutions at physiological pH: Role of nitrous anhydride and effects of phosphate and chloride
    • Lewis, R. S., Tannenbaum, S. R., and Dean, M. W. (1995) Kinetics of N-nitrosation in oxygenated nitric oxide solutions at physiological pH: Role of nitrous anhydride and effects of phosphate and chloride. J. Am. Chem. Soc. 117, 3933-3939.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3933-3939
    • Lewis, R.S.1    Tannenbaum, S.R.2    Dean, M.W.3
  • 20
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytoehrome P-450 type heme protein
    • White, K. A., and Marietta, M. A. (1992) Nitric oxide synthase is a cytoehrome P-450 type heme protein. Biochemistry 31, 6627-6631.
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marietta, M.A.2
  • 21
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J. R., and Marietta, M. A. (1994) Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marietta, M.A.2
  • 22
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • Sharma, V. S., Traylor, T. G., Gardiner, R., and Mizuka, H. (1987) Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry 26, 3837-3743.
    • (1987) Biochemistry , vol.26 , pp. 3837-13743
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizuka, H.4
  • 24
    • 0026038522 scopus 로고
    • Studies of the primary oxygen intermediate in the reaction of fully reduced cytoehrome oxidase
    • Blackmore, R. S., Greenwood, G., and Gibson, Q. H. (1991) Studies of the primary oxygen intermediate in the reaction of fully reduced cytoehrome oxidase. J. Biol. Chem. 266, 19245-19249.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19245-19249
    • Blackmore, R.S.1    Greenwood, G.2    Gibson, Q.H.3
  • 25
    • 10544224793 scopus 로고
    • Heme proteins, ligands, and quanta
    • Gibson, Q. H. (1989) Heme proteins, ligands, and quanta. J. Biol. Chem. 264, 20156-20158.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20156-20158
    • Gibson, Q.H.1
  • 26
    • 0025243607 scopus 로고    scopus 로고
    • Analysis of ligand binding to sperm whale myoglobin using site directed mutagenesis and laser photolysis techniques
    • 199
    • Carver, T. E., et al. (199) Analysis of ligand binding to sperm whale myoglobin using site directed mutagenesis and laser photolysis techniques. J. Biol. Chem. 265, 20007-20020.
    • J. Biol. Chem. , vol.265 , pp. 20007-20020
    • Carver, T.E.1
  • 27
    • 0025879748 scopus 로고
    • Ligand binding in a hierarchy of globin complexes. The hexagonal bilayer hemoglobin of Lumbricus terrestris and its heme containing subunits
    • Gibson, Q. H., et al. (1991) Ligand binding in a hierarchy of globin complexes. The hexagonal bilayer hemoglobin of Lumbricus terrestris and its heme containing subunits. J. Biol. Chem. 226, 13097-13102.
    • (1991) J. Biol. Chem. , vol.226 , pp. 13097-13102
    • Gibson, Q.H.1
  • 28
    • 0025734848 scopus 로고
    • Ligand binding and protein relaxation in hemeproteins: A room temperature analysis of nitric oxide geminate recombination
    • Petrich, J. W., et al. (1991) Ligand binding and protein relaxation in hemeproteins: A room temperature analysis of nitric oxide geminate recombination. Biochemistry 30, 3975-3987.
    • (1991) Biochemistry , vol.30 , pp. 3975-3987
    • Petrich, J.W.1
  • 29
    • 0000399717 scopus 로고
    • Photochemistry of nitric oxide adducts of water-soluble iron(III)-porphyrin and ferrihemoproteins studied by nanosecond laser photolysis
    • Hishino, M., Ozawa, K., Seki, H., and Ford, P. C. (1993) Photochemistry of nitric oxide adducts of water-soluble iron(III)-porphyrin and ferrihemoproteins studied by nanosecond laser photolysis. J. Am. Chem. Soc. 115, 9568-9575.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9568-9575
    • Hishino, M.1    Ozawa, K.2    Seki, H.3    Ford, P.C.4
  • 30
    • 0000277360 scopus 로고
    • Preparation and structural characterization of nitrosyl complexes of ferric porphyrinates. Molecular structure of aquonitrosyl (meso-tetraphenylporphinato) iron(III)perchlorate and nitrosyl (octaethylporphinato) iron(III)perchlorate
    • Scheldt, R. W., Lee, L. J., and Hatano, K. (1984) Preparation and structural characterization of nitrosyl complexes of ferric porphyrinates. Molecular structure of aquonitrosyl (meso-tetraphenylporphinato) iron(III)perchlorate and nitrosyl (octaethylporphinato) iron(III)perchlorate. J. Am. Chem. Soc. 99, 7315-7322.
    • (1984) J. Am. Chem. Soc. , vol.99 , pp. 7315-7322
    • Scheldt, R.W.1    Lee, L.J.2    Hatano, K.3
  • 31
    • 0025006512 scopus 로고
    • Redox reactivity of iron-(III)porphyrins and hemeproteins with nitric oxide. Nitrosyl transfer to carbon, nitrogen, oxygen and sulfur
    • Wade, R. S., and Castro, C. E. (1990) Redox reactivity of iron-(III)porphyrins and hemeproteins with nitric oxide. Nitrosyl transfer to carbon, nitrogen, oxygen and sulfur. Chem. Res. Toxicol. 3, 289-291.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 289-291
    • Wade, R.S.1    Castro, C.E.2
  • 32
    • 0028137022 scopus 로고
    • The interconversion of nucleic acid bases by iron(III)porphyrins and nitric oxide
    • Castro, C. E., and Bartnicki, E. W. (1994) The interconversion of nucleic acid bases by iron(III)porphyrins and nitric oxide. J. Org. Chem. 59, 4051-4052.
    • (1994) J. Org. Chem. , vol.59 , pp. 4051-4052
    • Castro, C.E.1    Bartnicki, E.W.2
  • 33
    • 10544253342 scopus 로고
    • Effects of Exposure to Nitrogen Dioxide
    • Effects of Exposure to Nitrogen Dioxide. (1994) Toxicology (Special Issue) 89, 1-320.
    • (1994) Toxicology (Special Issue) , vol.89 , pp. 1-320
  • 34
    • 0002886608 scopus 로고
    • Kinetics of reactive dissolutions of nitrogen oxides into aqueous solutions
    • (Schwartz, S. E., Ed.) John Wiley and Sons, New York
    • Schwartz, E., and White, W. H. (1983) Kinetics of reactive dissolutions of nitrogen oxides into aqueous solutions. In Trace Atmospheric Constituents, Properties, Transformation and Fates (Schwartz, S. E., Ed.) pp 1-117, John Wiley and Sons, New York.
    • (1983) Trace Atmospheric Constituents, Properties, Transformation and Fates , pp. 1-117
    • Schwartz, E.1    White, W.H.2
  • 35
    • 0011076031 scopus 로고
    • Hemoglobin and myoglobin
    • (Dolphin, D., Ed.) Chapter 10, Academic Press, New York
    • Ten Eyck, L. H. (1979) Hemoglobin and myoglobin. In The Porphyrins, Volume VII (Dolphin, D., Ed.) Chapter 10, pp 445-472, Academic Press, New York.
    • (1979) The Porphyrins , vol.7 , pp. 445-472
    • Ten Eyck, L.H.1
  • 36
    • 85050535788 scopus 로고
    • The chemistry of peroxynitrites
    • (Karlin, K. D., Ed.) John Wiley and Sons, New York
    • Edwards, J. O., and Plumb, R. C. (1994) The chemistry of peroxynitrites. In Progress in Inorganic Chemistry (Karlin, K. D., Ed.) Vol. 41, pp 599-635, John Wiley and Sons, New York.
    • (1994) Progress in Inorganic Chemistry , vol.41 , pp. 599-635
    • Edwards, J.O.1    Plumb, R.C.2
  • 37
    • 0026680555 scopus 로고
    • A stable solid that generates hydroxyl radicals upon dissolution in aqueous solution. Reaction with proteins and nucleic acids
    • King, P. A., Anderson, V. E., Edwards, J. O., Gustafson, G., Plumb, R. C., and Suggs, J. W. (1992) A stable solid that generates hydroxyl radicals upon dissolution in aqueous solution. Reaction with proteins and nucleic acids. J. Am. Chem. Soc. 114, 5430-5432.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5430-5432
    • King, P.A.1    Anderson, V.E.2    Edwards, J.O.3    Gustafson, G.4    Plumb, R.C.5    Suggs, J.W.6
  • 38
    • 0017800579 scopus 로고
    • Conversion of oxyhemoglobin to methemoglobin by organic and inorganic reductants
    • Castro, C. E., Wade, R. S., and Belser, N. O. (1978) Conversion of oxyhemoglobin to methemoglobin by organic and inorganic reductants. Biochemistry 17, 225-231.
    • (1978) Biochemistry , vol.17 , pp. 225-231
    • Castro, C.E.1    Wade, R.S.2    Belser, N.O.3
  • 40
    • 49749225196 scopus 로고
    • Determination of nitrate in sea water
    • Chow, T. J., and Johnstone, M. S. (1962) Determination of nitrate in sea water. Anal. Chem. Acta 27, 441-446.
    • (1962) Anal. Chem. Acta , vol.27 , pp. 441-446
    • Chow, T.J.1    Johnstone, M.S.2
  • 42
    • 0000537694 scopus 로고
    • Activation of nitrite ion by iron(III) porphyrins. Stoichiometric oxygentransfer to carbon, nitrogen phosphorous and sulfur
    • Castro, C. E., and O'Shea, S. K. (1995) Activation of nitrite ion by iron(III) porphyrins. Stoichiometric oxygentransfer to carbon, nitrogen phosphorous and sulfur. J. Org. Chem. 60, 1922-1923.
    • (1995) J. Org. Chem. , vol.60 , pp. 1922-1923
    • Castro, C.E.1    O'Shea, S.K.2
  • 43
    • 0029933010 scopus 로고    scopus 로고
    • Ozone from iron(III) porphyrin nitrite ion and oxygen
    • Castro, C. E. (1996) Ozone from iron(III) porphyrin nitrite ion and oxygen. J. Am. Chem. Soc. 118, 3894-3895.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3894-3895
    • Castro, C.E.1
  • 44
    • 0014691369 scopus 로고
    • Autoxidation of oxymyoglobins
    • Brown, W. D., and Mebine, L. B. (1969) Autoxidation of oxymyoglobins. J. Biol. Chem. 244, 6696-6701.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6696-6701
    • Brown, W.D.1    Mebine, L.B.2
  • 46
    • 0001672904 scopus 로고    scopus 로고
    • Selective Oxygen Transfers with Iron(III) Porphyrin Nitrite
    • O'Shea, S. K., Wang, W., Wade, R. S., and Castro, C. E. (1996) Selective Oxygen Transfers with Iron(III) Porphyrin Nitrite. J. Org. Chem. 61, 6388-6395.
    • (1996) J. Org. Chem. , vol.61 , pp. 6388-6395
    • O'Shea, S.K.1    Wang, W.2    Wade, R.S.3    Castro, C.E.4


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