메뉴 건너뛰기




Volumn 41, Issue 3, 2006, Pages 503-512

Reduction of manganese porphyrins by flavoenzymes and submitochondrial particles: A catalytic cycle for the reduction of peroxynitrite

Author keywords

Catalysis; Flavoenzyme; Manganese porphyrin; Mitochondria; Peroxynitrite

Indexed keywords

FLAVOPROTEIN; MANGANESE TETRAKIS[(N ETHYL)PYRIDINIUM 2 YL]PORPHYRIN; MANGANESE TETRAKIS[(N ETHYL)PYRIDINIUM 4 YL]PORPHYRIN; NITRITE; PEROXYNITRITE; PORPHYRIN DERIVATIVE; SUCCINATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 33745829019     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.04.028     Document Type: Article
Times cited : (74)

References (59)
  • 4
    • 0036667559 scopus 로고    scopus 로고
    • Inhibition of airway inflammation and hyperreactivity by an antioxidant mimetic
    • Chang L.Y., and Crapo J.D. Inhibition of airway inflammation and hyperreactivity by an antioxidant mimetic. Free Radic. Biol. Med. 33 (2002) 379-386
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 379-386
    • Chang, L.Y.1    Crapo, J.D.2
  • 6
    • 3242755872 scopus 로고    scopus 로고
    • Mouse spinal cord compression injury is ameliorated by intrathecal cationic manganese(III)porphyrin catalytic antioxidant therapy
    • Sheng H., Spasojevic I., Warner D.S., and Batinic-Haberle I. Mouse spinal cord compression injury is ameliorated by intrathecal cationic manganese(III)porphyrin catalytic antioxidant therapy. Neurosci. Lett. 366 (2004) 220-225
    • (2004) Neurosci. Lett. , vol.366 , pp. 220-225
    • Sheng, H.1    Spasojevic, I.2    Warner, D.S.3    Batinic-Haberle, I.4
  • 7
    • 4644317861 scopus 로고    scopus 로고
    • Antioxidant treatment reduces expansion and contraction of antigen-specific CD8+ T cells during primary but not secondary viral infection
    • Laniewski N.G., and Grayson J.M. Antioxidant treatment reduces expansion and contraction of antigen-specific CD8+ T cells during primary but not secondary viral infection. J. Virol. 78 (2004) 11246-11257
    • (2004) J. Virol. , vol.78 , pp. 11246-11257
    • Laniewski, N.G.1    Grayson, J.M.2
  • 8
    • 2942623947 scopus 로고    scopus 로고
    • Catalytic antioxidants: a radical approach to new therapeutics
    • Day B.J. Catalytic antioxidants: a radical approach to new therapeutics. Drug Discov. Today 9 (2004) 557-566
    • (2004) Drug Discov. Today , vol.9 , pp. 557-566
    • Day, B.J.1
  • 10
    • 0000363321 scopus 로고    scopus 로고
    • Relationship among redox potential, proton dissociation constants of pyrrolic nitrogens and in vivo and in vitro superoxide dismutating activities of manganese (III) an iron (III) water soluble porphyrins
    • Batinic-Haberle I., Spasojevic I., Hambright P., Benov L., Crumbliss A.L., and Fridovich I. Relationship among redox potential, proton dissociation constants of pyrrolic nitrogens and in vivo and in vitro superoxide dismutating activities of manganese (III) an iron (III) water soluble porphyrins. Inorg. Chem. 38 (1999) 4011-4022
    • (1999) Inorg. Chem. , vol.38 , pp. 4011-4022
    • Batinic-Haberle, I.1    Spasojevic, I.2    Hambright, P.3    Benov, L.4    Crumbliss, A.L.5    Fridovich, I.6
  • 11
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner K.M., Liochev S.I., and Fridovich I. Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo. J. Biol. Chem. 269 (1994) 23471-23476
    • (1994) J. Biol. Chem. , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 12
    • 0036124217 scopus 로고    scopus 로고
    • Manganese porphyrins and related compounds as mimics of superoxide dismutase
    • Batinic-Haberle I. Manganese porphyrins and related compounds as mimics of superoxide dismutase. Methods Enzymol. 349 (2002) 223-233
    • (2002) Methods Enzymol. , vol.349 , pp. 223-233
    • Batinic-Haberle, I.1
  • 13
    • 2942731654 scopus 로고    scopus 로고
    • New class of potent catalysts of O(2)[radical dot](-) dismutation. Mn(iii)ortho-methoxyethylpyridyl- and di-ortho-methoxyethylimidazolylporphyrins
    • Batinic-Haberle I., Spasojevic I., Stevens R.D., Hambright P., Neta P., Okado-Matsumoto A., and Fridovich I. New class of potent catalysts of O(2)[radical dot](-) dismutation. Mn(iii)ortho-methoxyethylpyridyl- and di-ortho-methoxyethylimidazolylporphyrins. Dalton Trans. (2004) 1696-1702
    • (2004) Dalton Trans. , pp. 1696-1702
    • Batinic-Haberle, I.1    Spasojevic, I.2    Stevens, R.D.3    Hambright, P.4    Neta, P.5    Okado-Matsumoto, A.6    Fridovich, I.7
  • 14
    • 0031573475 scopus 로고    scopus 로고
    • Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury
    • Day B.J., Fridovich I., and Crapo J.D. Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury. Arch. Biochem. Biophys. 347 (1997) 256-262
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 256-262
    • Day, B.J.1    Fridovich, I.2    Crapo, J.D.3
  • 15
    • 0343554032 scopus 로고    scopus 로고
    • Rapid decomposition of peroxynitrite by manganese porphyrin-antioxidant redox couples
    • Lee J., Hunt J.A., and Groves J.T. Rapid decomposition of peroxynitrite by manganese porphyrin-antioxidant redox couples. Bioorg. Med. Chem. Lett. 7 (1997) 2913-2918
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2913-2918
    • Lee, J.1    Hunt, J.A.2    Groves, J.T.3
  • 16
    • 0344348820 scopus 로고    scopus 로고
    • Catalytic scavenging of peroxynitrite by isomeric Mn(III) N- methylpyridylporphyrins in the presence of reductants
    • Ferrer-Sueta G., Batinic-Haberle I., Spasojevic I., Fridovich I., and Radi R. Catalytic scavenging of peroxynitrite by isomeric Mn(III) N- methylpyridylporphyrins in the presence of reductants. Chem. Res. Toxicol. 12 (1999) 442-449
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 442-449
    • Ferrer-Sueta, G.1    Batinic-Haberle, I.2    Spasojevic, I.3    Fridovich, I.4    Radi, R.5
  • 19
    • 0035503501 scopus 로고    scopus 로고
    • Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics
    • Melov S., Doctrow S.R., Schneider J.A., Haberson J., Patel M., Coskun P.E., Huffman K., Wallace D.C., and Malfroy B. Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics. J. Neurosci. 21 (2001) 8348-8353
    • (2001) J. Neurosci. , vol.21 , pp. 8348-8353
    • Melov, S.1    Doctrow, S.R.2    Schneider, J.A.3    Haberson, J.4    Patel, M.5    Coskun, P.E.6    Huffman, K.7    Wallace, D.C.8    Malfroy, B.9
  • 20
    • 0031977242 scopus 로고    scopus 로고
    • Molecular actions of a Mn(III)Porphyrin superoxide dismutase mimetic and peroxynitrite scavenger: reaction with nitric oxide and direct inhibition of NO synthase and soluble guanylyl cyclase
    • Pfeiffer S., Schrammel A., Koesling D., Schmidt K., and Mayer B. Molecular actions of a Mn(III)Porphyrin superoxide dismutase mimetic and peroxynitrite scavenger: reaction with nitric oxide and direct inhibition of NO synthase and soluble guanylyl cyclase. Mol. Pharmacol. 53 (1998) 795-800
    • (1998) Mol. Pharmacol. , vol.53 , pp. 795-800
    • Pfeiffer, S.1    Schrammel, A.2    Koesling, D.3    Schmidt, K.4    Mayer, B.5
  • 21
    • 0344255591 scopus 로고    scopus 로고
    • Flavin-dependent antioxidant properties of a new series of meso-N,N′-dialkyl-imidazolium substituted manganese(III) porphyrins
    • Kachadourian R., Johnson C.A., Min E., Spasojevic I., and Day B.J. Flavin-dependent antioxidant properties of a new series of meso-N,N′-dialkyl-imidazolium substituted manganese(III) porphyrins. Biochem. Pharmacol. 67 (2004) 77-85
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 77-85
    • Kachadourian, R.1    Johnson, C.A.2    Min, E.3    Spasojevic, I.4    Day, B.J.5
  • 23
    • 0033574624 scopus 로고    scopus 로고
    • Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide [published erratum appears in J. Biol. Chem. 274(2):19508; 19990
    • Bonini M.G., Radi R., Ferrer-Sueta G., Ferreira A.M., and Augusto O. Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide [published erratum appears in J. Biol. Chem. 274(2):19508; 19990. J. Biol. Chem. 274 (1999) 10802-10806
    • (1999) J. Biol. Chem. , vol.274 , pp. 10802-10806
    • Bonini, M.G.1    Radi, R.2    Ferrer-Sueta, G.3    Ferreira, A.M.4    Augusto, O.5
  • 24
    • 0036122570 scopus 로고    scopus 로고
    • Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite
    • Ferrer-Sueta G., Quijano C., Alvarez B., and Radi R. Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite. Methods Enzymol. 349 (2002) 23-37
    • (2002) Methods Enzymol. , vol.349 , pp. 23-37
    • Ferrer-Sueta, G.1    Quijano, C.2    Alvarez, B.3    Radi, R.4
  • 26
    • 0032486758 scopus 로고    scopus 로고
    • Mechanism of iron porphyrin reactions with peroxynitrite
    • Lee J., Hunt J.A., and Groves J.T. Mechanism 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.1    Hunt, J.A.2    Groves, J.T.3
  • 27
  • 29
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger T., Budde H., Flohe L., Menge U., Singh M., Trujillo M., and Radi R. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423 (2004) 182-191
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 182-191
    • Jaeger, T.1    Budde, H.2    Flohe, L.3    Menge, U.4    Singh, M.5    Trujillo, M.6    Radi, R.7
  • 30
    • 4544264011 scopus 로고    scopus 로고
    • Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols
    • Trujillo M., Budde H., Pineyro M.D., Stehr M., Robello C., Flohe L., and Radi R. Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. J. Biol. Chem. 279 (2004) 34175-34182
    • (2004) J. Biol. Chem. , vol.279 , pp. 34175-34182
    • Trujillo, M.1    Budde, H.2    Pineyro, M.D.3    Stehr, M.4    Robello, C.5    Flohe, L.6    Radi, R.7
  • 31
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R., Griffin P., and Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407 (2000) 211-215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 32
    • 3042632985 scopus 로고    scopus 로고
    • Tetrahydrobiopterin rapidly reduces the SOD mimic Mn(III) ortho-tetrakis(N-ethylpyridinium-2-yl)porphyrin
    • Batinic-Haberle I., Spasojevic I.I., and Fridovich I. Tetrahydrobiopterin rapidly reduces the SOD mimic Mn(III) ortho-tetrakis(N-ethylpyridinium-2-yl)porphyrin. Free Radic. Biol. Med. 37 (2004) 367-374
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 367-374
    • Batinic-Haberle, I.1    Spasojevic, I.I.2    Fridovich, I.3
  • 33
    • 0032544579 scopus 로고    scopus 로고
    • The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium- 2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic
    • Batinic-Haberle I., Benov L., Spasojevic I., and Fridovich I. The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium- 2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic. J. Biol. Chem. 273 (1998) 24521-24528
    • (1998) J. Biol. Chem. , vol.273 , pp. 24521-24528
    • Batinic-Haberle, I.1    Benov, L.2    Spasojevic, I.3    Fridovich, I.4
  • 35
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., Beckman J.S., Bush K.M., and Freeman B.A. 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
  • 36
    • 0001889165 scopus 로고
    • Sub-fractionation of mitochondria and isolation of the proteins of oxidative phosphorylation
    • Darley-Usmar V.M., Rickwood D., and Wilson M.T. (Eds), IRL Press, Oxford
    • Ragan I., Wilson M.T., Darley-Usmar V.M., and Lowe P.N. Sub-fractionation of mitochondria and isolation of the proteins of oxidative phosphorylation. In: Darley-Usmar V.M., Rickwood D., and Wilson M.T. (Eds). Mitochondria A Practical Approach (1987), IRL Press, Oxford 79-112
    • (1987) Mitochondria A Practical Approach , pp. 79-112
    • Ragan, I.1    Wilson, M.T.2    Darley-Usmar, V.M.3    Lowe, P.N.4
  • 37
    • 0027370376 scopus 로고
    • GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems
    • Mendes P. GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems. Comput. Appl. Biosci. 9 (1993) 563-571
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 563-571
    • Mendes, P.1
  • 38
    • 0030921160 scopus 로고    scopus 로고
    • Biochemistry by numbers: simulation of biochemical pathways with Gepasi 3
    • Mendes P. Biochemistry by numbers: simulation of biochemical pathways with Gepasi 3. Trends Biochem. Sci. 22 (1997) 361-363
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 361-363
    • Mendes, P.1
  • 39
    • 0005030169 scopus 로고
    • The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system
    • Martonosi A.V. (Ed), Plenum, New York
    • Hatefi Y. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi A.V. (Ed). The enzymes of biological membranes vol. 4 (1976), Plenum, New York 3-41
    • (1976) The enzymes of biological membranes , vol.4 , pp. 3-41
    • Hatefi, Y.1
  • 40
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54 (1985) 1015-1069
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 41
    • 77956839772 scopus 로고
    • Progress in Succinate: quinone oxidoreductase research
    • Neuberger A., and van Deenen L.L.M. (Eds), Elsevier Science, Amsterdam
    • Hederstedt L., and Ohnishi T. Progress in Succinate: quinone oxidoreductase research. In: Neuberger A., and van Deenen L.L.M. (Eds). New comprehensive biochemistry vol. 23 (1992), Elsevier Science, Amsterdam 163-198
    • (1992) New comprehensive biochemistry , vol.23 , pp. 163-198
    • Hederstedt, L.1    Ohnishi, T.2
  • 42
    • 0033351343 scopus 로고    scopus 로고
    • Electrochemical characterization and electrocatalysis of high valent manganese meso-tetrakis(N-methyl-2-pyridyl)porphyrin
    • Chen F., Cheng S., Yu C., Liu M., and Su Y.O. Electrochemical characterization and electrocatalysis of high valent manganese meso-tetrakis(N-methyl-2-pyridyl)porphyrin. J. Electroanal. Chem. 474 (1999) 52-59
    • (1999) J. Electroanal. Chem. , vol.474 , pp. 52-59
    • Chen, F.1    Cheng, S.2    Yu, C.3    Liu, M.4    Su, Y.O.5
  • 43
    • 0028260775 scopus 로고
    • Peroxynitrite inactivates thiol-containing enzymes of Trypanosoma cruzi energetic metabolism and inhibits cell respiration
    • Rubbo H., Denicola A., and Radi R. Peroxynitrite inactivates thiol-containing enzymes of Trypanosoma cruzi energetic metabolism and inhibits cell respiration. Arch. Biochem. Biophys. 308 (1994) 96-102
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 96-102
    • Rubbo, H.1    Denicola, A.2    Radi, R.3
  • 44
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A., and Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch. Biochem. Biophys. 328 (1996) 309-316
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 45
  • 46
    • 0344255591 scopus 로고    scopus 로고
    • Flavin-dependent antioxidant properties of a new series of meso-N,N′-dialkylimidazolium substituted manganese(III) porphyrins
    • Kachadourian R., Johnson C.A., Min E., Spasojevic I., and Day B.J. Flavin-dependent antioxidant properties of a new series of meso-N,N′-dialkylimidazolium substituted manganese(III) porphyrins. Biochem. Pharmacol. 67 (2004) 77-85
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 77-85
    • Kachadourian, R.1    Johnson, C.A.2    Min, E.3    Spasojevic, I.4    Day, B.J.5
  • 47
    • 0027990677 scopus 로고
    • Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Sled V.D., Rudnitzky N.I., Hatefi Y., and Ohnishi T. Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I). Biochemistry 33 (1994) 10069-10075
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 48
    • 0343052744 scopus 로고    scopus 로고
    • Succinate: quinone oxidoreductases. Variations on a conserved theme
    • Hagerhall C. Succinate: quinone oxidoreductases. Variations on a conserved theme. Biochim. Biophys. Acta 1320 (1997) 107-141
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hagerhall, C.1
  • 50
    • 0001639468 scopus 로고
    • Approximations in the kinetics of consecutive reactions
    • McDaniel H.H., and Smoot C.R. Approximations in the kinetics of consecutive reactions. J. Phys. Chem. 60 (1956) 966-969
    • (1956) J. Phys. Chem. , vol.60 , pp. 966-969
    • McDaniel, H.H.1    Smoot, C.R.2
  • 56
    • 0034883512 scopus 로고    scopus 로고
    • Dependence of excitotoxic neurodegeneration on mitochondrial aconitase inactivation
    • Li Q.Y., Pedersen C., Day B.J., and Patel M. Dependence of excitotoxic neurodegeneration on mitochondrial aconitase inactivation. J. Neurochem. 78 (2001) 746-755
    • (2001) J. Neurochem. , vol.78 , pp. 746-755
    • Li, Q.Y.1    Pedersen, C.2    Day, B.J.3    Patel, M.4
  • 57
    • 20444392739 scopus 로고    scopus 로고
    • Interactions of mitochondria-targeted and untargeted ubiquinones with the mitochondrial respiratory chain and reactive oxygen species. Implications for the use of exogenous ubiquinones as therapies and experimental tools
    • James A.M., Cocheme H.M., Smith R.A., and Murphy M.P. Interactions of mitochondria-targeted and untargeted ubiquinones with the mitochondrial respiratory chain and reactive oxygen species. Implications for the use of exogenous ubiquinones as therapies and experimental tools. J. Biol. Chem. 280 (2005) 21295-21312
    • (2005) J. Biol. Chem. , vol.280 , pp. 21295-21312
    • James, A.M.1    Cocheme, H.M.2    Smith, R.A.3    Murphy, M.P.4
  • 59
    • 0010436289 scopus 로고
    • Photochemistry of manganese porphyrins. Part 3. Interconversion of MnII/MnIII
    • Duncan I.A., Harriman A., and Porter G. Photochemistry of manganese porphyrins. Part 3. Interconversion of MnII/MnIII. J. Chem. Soc. Faraday Trans. II 76 (1980) 1415
    • (1980) J. Chem. Soc. Faraday Trans. II , vol.76 , pp. 1415
    • Duncan, I.A.1    Harriman, A.2    Porter, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.