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Volumn 53, Issue 10, 2012, Pages 1819-1828

Protection against peroxynitrite by pseudoperoxidase from Leishmania major

Author keywords

Free radicals; Heme protein; Leishmania; Membrane; Peroxynitrite

Indexed keywords

ANTIOXIDANT; HEMOPROTEIN; LEISHMANIA MAJOR PSEUDOPEROXIDASE; PEROXYNITRITE; UNCLASSIFIED DRUG;

EID: 84867390915     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.08.583     Document Type: Article
Times cited : (11)

References (53)
  • 2
    • 0033557291 scopus 로고    scopus 로고
    • Macrophage microbicidal mechanisms in vivo: Reactive nitrogen versus oxygen intermediates in the killing of intracellular visceral Leishmania donovani
    • H.W. Murray, and C.F. Nathan Macrophage microbicidal mechanisms in vivo: reactive nitrogen versus oxygen intermediates in the killing of intracellular visceral Leishmania donovani J. Exp. Med 189 1999 741 746
    • (1999) J. Exp. Med , vol.189 , pp. 741-746
    • Murray, H.W.1    Nathan, C.F.2
  • 3
    • 0019978017 scopus 로고
    • Cell-mediated immune response in experimental visceral leishmaniasis. II. Oxygen-dependent killing of intracellular Leishmania donovani amastigotes
    • H.W. Murray Cell-mediated immune response in experimental visceral leishmaniasis. II. Oxygen-dependent killing of intracellular Leishmania donovani amastigotes J. Immunol 129 1982 351 357
    • (1982) J. Immunol , vol.129 , pp. 351-357
    • Murray, H.W.1
  • 4
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • C. Nathan, and M.U. Shiloh Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens Proc. Natl. Acad. Sci. USA 97 2000 8841 8848
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 5
    • 0031570501 scopus 로고    scopus 로고
    • Host/pathogen interactions: Mechanisms of nitric oxide-related antimicrobial activity
    • F.C. Fang Host/pathogen interactions: mechanisms of nitric oxide-related antimicrobial activity J. Clin. Invest. 99 1997 2818 2825
    • (1997) J. Clin. Invest. , vol.99 , pp. 2818-2825
    • Fang, F.C.1
  • 6
    • 0035823608 scopus 로고    scopus 로고
    • Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi: Evidence for an enzymatic detoxification of hydroxyl radicals
    • S.D. Barr, and L. Gedamu Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi: evidence for an enzymatic detoxification of hydroxyl radicals J. Biol. Chem 276 2001 34279 34287
    • (2001) J. Biol. Chem , vol.276 , pp. 34279-34287
    • Barr, S.D.1    Gedamu, L.2
  • 7
    • 25144484821 scopus 로고    scopus 로고
    • Leishmania major encodes an unusual peroxidase that is a close homologue of plant ascorbate peroxidase: A novel role of the transmembrane domain
    • S. Adak, and A.K. Datta Leishmania major encodes an unusual peroxidase that is a close homologue of plant ascorbate peroxidase: a novel role of the transmembrane domain Biochem. J 390 2005 465 474
    • (2005) Biochem. J , vol.390 , pp. 465-474
    • Adak, S.1    Datta, A.K.2
  • 8
    • 19344372534 scopus 로고    scopus 로고
    • Distinct overexpression of cytosolic and mitochondrial tryparedoxin peroxidases results in preferential detoxification of different oxidants in arsenite-resistant Leishmania amazonensis with and without DNA amplification
    • Y.C. Lin, J.Y. Hsu, S.C. Chiang, and S.T. Lee Distinct overexpression of cytosolic and mitochondrial tryparedoxin peroxidases results in preferential detoxification of different oxidants in arsenite-resistant Leishmania amazonensis with and without DNA amplification Mol. Biochem. Parasitol 142 2005 66 75
    • (2005) Mol. Biochem. Parasitol , vol.142 , pp. 66-75
    • Lin, Y.C.1    Hsu, J.Y.2    Chiang, S.C.3    Lee, S.T.4
  • 9
    • 10444255569 scopus 로고    scopus 로고
    • Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity
    • T.J. Vickers, S. Wyllie, and A.H. Fairlamb Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity J. Biol. Chem. 279 2004 49003 49009
    • (2004) J. Biol. Chem. , vol.279 , pp. 49003-49009
    • Vickers, T.J.1    Wyllie, S.2    Fairlamb, A.H.3
  • 10
    • 0037328022 scopus 로고    scopus 로고
    • Role of superoxide dismutase in survival of Leishmania within the macrophage
    • S. Ghosh, S. Goswami, and S. Adhya Role of superoxide dismutase in survival of Leishmania within the macrophage Biochem. J. 369 2003 447 452
    • (2003) Biochem. J. , vol.369 , pp. 447-452
    • Ghosh, S.1    Goswami, S.2    Adhya, S.3
  • 11
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls: The cytotoxic potential of superoxide and nitric oxide
    • R. Radi, J.S. Beckman, K.M. Bush, and B.A. Freeman Peroxynitrite oxidation of sulfhydryls: the cytotoxic potential of superoxide and nitric oxide J. Biol. Chem. 266 1991 4244 4250
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 12
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • J.S. Beckman, T.W. Beckman, J. Chen, P.A. Marshall, and B.A. Freeman Apparent hydroxyl radical production by peroxynitrite: 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
  • 13
    • 64749101531 scopus 로고    scopus 로고
    • Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
    • G. Ferrer-Sueta, and R. Radi Chemical biology of peroxynitrite: kinetics, diffusion, and radicals ACS Chem. Biol. 4 2009 161 177
    • (2009) ACS Chem. Biol. , vol.4 , pp. 161-177
    • Ferrer-Sueta, G.1    Radi, R.2
  • 15
    • 0027303364 scopus 로고
    • Interaction of myeloperoxidase with peroxynitrite: A comparison with lactoperoxidase, horseradish peroxidase and catalase
    • R. Floris, S.R. Piersma, G. Yang, P. Jones, and R. Wever Interaction of myeloperoxidase with peroxynitrite: a comparison with lactoperoxidase, horseradish peroxidase and catalase Eur. J. Biochem. 215 1993 767 775
    • (1993) Eur. J. Biochem. , vol.215 , pp. 767-775
    • Floris, R.1    Piersma, S.R.2    Yang, G.3    Jones, P.4    Wever, R.5
  • 16
    • 0033678831 scopus 로고    scopus 로고
    • Nitration and inactivation of cytochrome P450BM-3 by peroxynitrite: Stopped-flow measurements prove ferryl intermediates
    • A. Daiber, S. Herold, C. Schoneich, D. Namgaladze, J.A. Peterson, and V. Ullrich Nitration and inactivation of cytochrome P450BM-3 by peroxynitrite: stopped-flow measurements prove ferryl intermediates Eur. J. Biochem. 267 2000 6729 6739
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6729-6739
    • Daiber, A.1    Herold, S.2    Schoneich, C.3    Namgaladze, D.4    Peterson, J.A.5    Ullrich, V.6
  • 17
    • 53549099423 scopus 로고    scopus 로고
    • Spectra and kinetic studies of the compound i derivative of cytochrome P450 119
    • X. Sheng, J.H. Horner, and M. Newcomb Spectra and kinetic studies of the compound I derivative of cytochrome P450 119 J. Am. Chem. Soc. 130 2008 13310 13320
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13310-13320
    • Sheng, X.1    Horner, J.H.2    Newcomb, M.3
  • 18
    • 3042771981 scopus 로고    scopus 로고
    • Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants
    • S. Herold, S. Kalinga, T. Matsui, and Y. Watanabe Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants J. Am. Chem. Soc. 126 2004 6945 6955
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6945-6955
    • Herold, S.1    Kalinga, S.2    Matsui, T.3    Watanabe, Y.4
  • 19
    • 0032486758 scopus 로고    scopus 로고
    • Mechanisms of iron porphyrin reactions with peroxynitrite
    • J.B. Lee, J.A. Hunt, and J.T. Groves Mechanisms of iron porphyrin reactions with peroxynitrite J. Am. Chem. Soc. 120 1998 7493 7501
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7493-7501
    • Lee, J.B.1    Hunt, J.A.2    Groves, J.T.3
  • 20
    • 34347339518 scopus 로고    scopus 로고
    • Comparative genomic analysis of three Leishmania species that cause diverse human disease
    • C.S. Peacock, K. Seeger, D. Harris, L. Murphy, and J.C. Ruiz Comparative genomic analysis of three Leishmania species that cause diverse human disease Nat. Genet. 39 2007 839 847
    • (2007) Nat. Genet. , vol.39 , pp. 839-847
    • Peacock, C.S.1    Seeger, K.2    Harris, D.3    Murphy, L.4    Ruiz, J.C.5
  • 22
    • 0036260085 scopus 로고    scopus 로고
    • Structure-function relationships in heme-proteins
    • M. Paoli, J. Marles-Wright, and A. Smith Structure-function relationships in heme-proteins DNA Cell Biol. 21 2002 271 280
    • (2002) DNA Cell Biol. , vol.21 , pp. 271-280
    • Paoli, M.1    Marles-Wright, J.2    Smith, A.3
  • 23
    • 0002548867 scopus 로고    scopus 로고
    • Heme: The most versatile redox centre in biology?
    • S.K. Chapman, S. Daff, and A.W. Munro Heme: the most versatile redox centre in biology? Struct. Bonding 88 1997 39 70
    • (1997) Struct. Bonding , vol.88 , pp. 39-70
    • Chapman, S.K.1    Daff, S.2    Munro, A.W.3
  • 24
    • 0027421337 scopus 로고
    • Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound i
    • J.E. Erman, L.B. Vitello, M.A. Miller, A. Shaw, K.A. Brown, and J. Kraut Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I Biochemistry 32 1993 9798 9806
    • (1993) Biochemistry , vol.32 , pp. 9798-9806
    • Erman, J.E.1    Vitello, L.B.2    Miller, M.A.3    Shaw, A.4    Brown, K.A.5    Kraut, J.6
  • 27
    • 56249117981 scopus 로고    scopus 로고
    • Leishmania major ascorbate peroxidase overexpression protects cells against reactive oxygen species-mediated cardiolipin oxidation
    • S. Dolai, R.K. Yadav, S. Pal, and S. Adak Leishmania major ascorbate peroxidase overexpression protects cells against reactive oxygen species-mediated cardiolipin oxidation Free Radic. Biol. Med. 45 2008 1520 1529
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1520-1529
    • Dolai, S.1    Yadav, R.K.2    Pal, S.3    Adak, S.4
  • 28
    • 77955295646 scopus 로고    scopus 로고
    • Ascorbate peroxidase from Leishmania major controls the virulence of infective stage of promastigotes by regulating oxidative stress
    • S. Pal, S. Dolai, R.K. Yadav, and S. Adak Ascorbate peroxidase from Leishmania major controls the virulence of infective stage of promastigotes by regulating oxidative stress PLoS One 5 2010 e11271
    • (2010) PLoS One , vol.5 , pp. 11271
    • Pal, S.1    Dolai, S.2    Yadav, R.K.3    Adak, S.4
  • 29
    • 41949126490 scopus 로고    scopus 로고
    • Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major - Kinetic studies on Trp208Phe mutant and wild type enzyme
    • R.K. Yadav, S. Dolai, S. Pal, and S. Adak Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major - kinetic studies on Trp208Phe mutant and wild type enzyme Biochim. Biophys. Acta 1784 2008 863 871
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 863-871
    • Yadav, R.K.1    Dolai, S.2    Pal, S.3    Adak, S.4
  • 30
    • 0027255711 scopus 로고
    • Glycosphingolipid antigens of Leishmania (Leishmania) amazonensis amastigotes identified by use of a monoclonal antibody
    • C.L. Barbieri, S. Giorgio, A.J. Merjan, and E.N. Figueiredo Glycosphingolipid antigens of Leishmania (Leishmania) amazonensis amastigotes identified by use of a monoclonal antibody Infect. Immun. 61 1993 2131 2137
    • (1993) Infect. Immun. , vol.61 , pp. 2131-2137
    • Barbieri, C.L.1    Giorgio, S.2    Merjan, A.J.3    Figueiredo, E.N.4
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem 72 1976 248 254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen)
    • K.G. Paul, H. Theorell, and A. Akeson The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen) Acta Chem. Scand. 7 1953 1284 1287
    • (1953) Acta Chem. Scand. , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 33
    • 33845872332 scopus 로고    scopus 로고
    • Effect of thiocyanate on the peroxidase and pseudocatalase activities of Leishmania major ascorbate peroxidase
    • S. Dolai, R.K. Yadav, A.K. Datta, and S. Adak Effect of thiocyanate on the peroxidase and pseudocatalase activities of Leishmania major ascorbate peroxidase Biochim. Biophys. Acta 1770 2007 247 256
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 247-256
    • Dolai, S.1    Yadav, R.K.2    Datta, A.K.3    Adak, S.4
  • 34
    • 0029688736 scopus 로고    scopus 로고
    • Synthesis of pure tetramethylammonium peroxynitrite
    • D.S. Bohle, P.A. Glassbrenner, and B. Hansert Synthesis of pure tetramethylammonium peroxynitrite Methods Enzymol. 269 1996 302 311
    • (1996) Methods Enzymol. , vol.269 , pp. 302-311
    • Bohle, D.S.1    Glassbrenner, P.A.2    Hansert, B.3
  • 35
    • 0032031965 scopus 로고    scopus 로고
    • The critical role of HEPES in SIN-1 cytotoxicity, peroxynitrite versus hydrogen peroxide
    • E.E. Lomonosova, M. Kirsch, U. Rauen, and H.D. Droot The critical role of HEPES in SIN-1 cytotoxicity, peroxynitrite versus hydrogen peroxide Free Radic. Biol. Med. 24 1998 522 528
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 522-528
    • Lomonosova, E.E.1    Kirsch, M.2    Rauen, U.3    Droot, H.D.4
  • 36
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O. Emanuelsson, H. Nielsen, S. Brunak, and G. von Heijne Predicting subcellular localization of proteins based on their N-terminal amino acid sequence J. Mol. Biol. 300 2000 1005 1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 37
    • 77249113196 scopus 로고    scopus 로고
    • Role of C-terminal acidic cluster in stabilization of heme spin state of ascorbate peroxidase from Leishmania major
    • R.K. Yadav, S. Dolai, S. Pal, and S. Adak Role of C-terminal acidic cluster in stabilization of heme spin state of ascorbate peroxidase from Leishmania major Arch. Biochem. Biophys. 495 2010 129 135
    • (2010) Arch. Biochem. Biophys. , vol.495 , pp. 129-135
    • Yadav, R.K.1    Dolai, S.2    Pal, S.3    Adak, S.4
  • 38
    • 8344231645 scopus 로고    scopus 로고
    • Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA
    • R.W. Clark, H. Youn, R.B. Parks, M.M. Cherney, G.P. Roberts, and J.N. Burstyn Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA Biochemistry 43 2004 14149 14160
    • (2004) Biochemistry , vol.43 , pp. 14149-14160
    • Clark, R.W.1    Youn, H.2    Parks, R.B.3    Cherney, M.M.4    Roberts, G.P.5    Burstyn, J.N.6
  • 39
    • 0027142050 scopus 로고
    • Structurally engineered cytochromes with unusual ligand-binding properties: Expression of Saccharomyces cerevisiae Met-80→Ala iso-1-cytochrome c
    • Y. Lu, D.R. Casimiro, K.L. Bren, J.H. Richards, and H.B. Gray Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met-80→Ala iso-1-cytochrome c Proc. Natl. Acad. Sci. USA 90 1993 11456 11459
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11456-11459
    • Lu, Y.1    Casimiro, D.R.2    Bren, K.L.3    Richards, J.H.4    Gray, H.B.5
  • 40
    • 0020478791 scopus 로고
    • Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes: Identification of the ligand trans to cysteinate in the native enzyme
    • J.H. Dawson, L.A. Andersson, and M. Sono Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes: identification of the ligand trans to cysteinate in the native enzyme J. Biol. Chem 257 1982 3606 3617
    • (1982) J. Biol. Chem , vol.257 , pp. 3606-3617
    • Dawson, J.H.1    Andersson, L.A.2    Sono, M.3
  • 42
    • 0032475847 scopus 로고    scopus 로고
    • Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA
    • S. Aono, K. Ohkubo, T. Matsuo, and H. Nakajima Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA J. Biol. Chem. 273 1998 25757 25764
    • (1998) J. Biol. Chem. , vol.273 , pp. 25757-25764
    • Aono, S.1    Ohkubo, K.2    Matsuo, T.3    Nakajima, H.4
  • 43
    • 2842546487 scopus 로고
    • Structural correlations and the vinyl influences in resonance Raman spectra of protoheme complexes and proteins
    • S. Choi, T.G. Spiro, K.C. Langry, K.N. Smith, D.L. Budd, and G.N. LaMar Structural correlations and the vinyl influences in resonance Raman spectra of protoheme complexes and proteins J. Am. Chem. Soc. 104 1982 4345 4351
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.C.3    Smith, K.N.4    Budd, D.L.5    Lamar, G.N.6
  • 44
    • 0017310256 scopus 로고
    • Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering
    • T. Kitagawa, Y. Kyogoku, T. Iizuka, and M.I. Saito Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering J. Am. Chem. Soc. 98 1976 5169 5173
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 5169-5173
    • Kitagawa, T.1    Kyogoku, Y.2    Iizuka, T.3    Saito, M.I.4
  • 45
    • 0024545028 scopus 로고
    • Structural characterization of cytochrome c peroxidase by resonance Raman scattering
    • S. Dasgupta, D.L. Rousseau., H. Anni, and T. Yonetani Structural characterization of cytochrome c peroxidase by resonance Raman scattering J. Biol. Chem. 264 1989 654 662
    • (1989) J. Biol. Chem. , vol.264 , pp. 654-662
    • Dasgupta, S.1    Rousseau, D.L.2    Anni, H.3    Yonetani, T.4
  • 46
    • 0028204437 scopus 로고
    • Characterization of polymer release from the flagellar pocket of Leishmania mexicana promastigotes
    • Y.D. Stierhof, T. Ilg, D.G. Russell, H. Hohenberg, and P. Overath Characterization of polymer release from the flagellar pocket of Leishmania mexicana promastigotes J. Cell Biol. 125 1994 321 331
    • (1994) J. Cell Biol. , vol.125 , pp. 321-331
    • Stierhof, Y.D.1    Ilg, T.2    Russell, D.G.3    Hohenberg, H.4    Overath, P.5
  • 47
    • 1642586813 scopus 로고    scopus 로고
    • Proteophosphoglycans of Leishmania mexicana: Identification, purification, structural and ultrastructural characterization of the secreted promastigote proteophosphoglycan pPPG2, a stage-specific glycoisoform of amastigote aPPG
    • C. Klein, U. Gopfert, N. Goehring, Y.D. Stierhof, and T. Ilg Proteophosphoglycans of Leishmania mexicana: identification, purification, structural and ultrastructural characterization of the secreted promastigote proteophosphoglycan pPPG2, a stage-specific glycoisoform of amastigote aPPG Biochem. J. 344 1999 775 786
    • (1999) Biochem. J. , vol.344 , pp. 775-786
    • Klein, C.1    Gopfert, U.2    Goehring, N.3    Stierhof, Y.D.4    Ilg, T.5
  • 48
    • 77954377299 scopus 로고    scopus 로고
    • Localization and induction of the A2 virulence factor in Leishmania: Evidence that A2 is a stress response protein
    • L.I. McCall, and G. Matlashewski Localization and induction of the A2 virulence factor in Leishmania: evidence that A2 is a stress response protein Mol. Microbiol 77 2010 518 530
    • (2010) Mol. Microbiol , vol.77 , pp. 518-530
    • McCall, L.I.1    Matlashewski, G.2
  • 49
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • P.R. Gardner Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases J. Inorg. Biochem. 99 2005 247 266
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 247-266
    • Gardner, P.R.1
  • 50
    • 0035964364 scopus 로고    scopus 로고
    • Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen
    • A. Hausladen, A. Gow, and J.S. Stamler Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen Proc. Natl. Acad. Sci. USA 98 2001 10108 10112
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10108-10112
    • Hausladen, A.1    Gow, A.2    Stamler, J.S.3
  • 53
    • 0032503059 scopus 로고    scopus 로고
    • Scavenging of peroxynitrite by a phenolic/peroxidase system prevents oxidative damage to DNA
    • S.C. Grace, M.G. Salgo, and W.A. Pryor Scavenging of peroxynitrite by a phenolic/peroxidase system prevents oxidative damage to DNA FEBS Lett 426 1998 24 28
    • (1998) FEBS Lett , vol.426 , pp. 24-28
    • Grace, S.C.1    Salgo, M.G.2    Pryor, W.A.3


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