메뉴 건너뛰기




Volumn 44, Issue 7, 2008, Pages 1406-1419

A mitochondria-targeted nitroxide is reduced to its hydroxylamine by ubiquinol in mitochondria

Author keywords

Mitochondria targeting; Nitroxide; TEMPOL; Triphenylphosphonium; Ubiquinol

Indexed keywords

HYDROGEN; HYDROXYLAMINE; NITROXIDE; ORGANIC SOLVENT; PHOSPHONIUM DERIVATIVE; PIPERIDINE DERIVATIVE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE;

EID: 40949161089     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.12.036     Document Type: Article
Times cited : (218)

References (65)
  • 2
    • 0034595909 scopus 로고    scopus 로고
    • The effects of Tempol on ferritin synthesis and Fe metabolism in lens epithelial cells
    • Goralska M., Holley B., and McGahan M.C. The effects of Tempol on ferritin synthesis and Fe metabolism in lens epithelial cells. Biochim. Biophys. Acta 1497 (2000) 51-60
    • (2000) Biochim. Biophys. Acta , vol.1497 , pp. 51-60
    • Goralska, M.1    Holley, B.2    McGahan, M.C.3
  • 4
    • 25644445936 scopus 로고    scopus 로고
    • Neuroprotective effects of TEMPOL in central and peripheral nervous system models of Parkinson's disease
    • Liang Q., Smith A.D., Pan S., Tyurin V.A., Kagan V.E., Hastings T.G., and Schor N.F. Neuroprotective effects of TEMPOL in central and peripheral nervous system models of Parkinson's disease. Biochem. Pharmacol. 70 (2005) 1371-1381
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1371-1381
    • Liang, Q.1    Smith, A.D.2    Pan, S.3    Tyurin, V.A.4    Kagan, V.E.5    Hastings, T.G.6    Schor, N.F.7
  • 8
    • 0037438769 scopus 로고    scopus 로고
    • Site-activity relationship of nitroxide radical's antioxidative effect
    • Samuni A.M., and Barenholz Y. Site-activity relationship of nitroxide radical's antioxidative effect. Free Radic. Biol. Med. 34 (2003) 177-185
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 177-185
    • Samuni, A.M.1    Barenholz, Y.2
  • 12
    • 0027194813 scopus 로고
    • Antioxidant activity of nitroxide radicals in lipid peroxidation of rat liver microsomes
    • Miura Y., Utsumi H., and Hamada A. Antioxidant activity of nitroxide radicals in lipid peroxidation of rat liver microsomes. Arch. Biochem. Biophys. 300 (1993) 148-156
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 148-156
    • Miura, Y.1    Utsumi, H.2    Hamada, A.3
  • 15
    • 0033056467 scopus 로고    scopus 로고
    • Kinetics of superoxide-induced exchange among nitroxide antioxidants and their oxidized and reduced forms
    • Zhang R., Goldstein S., and Samuni A. Kinetics of superoxide-induced exchange among nitroxide antioxidants and their oxidized and reduced forms. Free Radic. Biol. Med. 26 (1999) 1245-1252
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 1245-1252
    • Zhang, R.1    Goldstein, S.2    Samuni, A.3
  • 16
    • 0026731503 scopus 로고
    • Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical
    • Voest E.E., van Faassen E., van Asbeck B.S., Neijt J.P., and Marx J.J. Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical. Biochim. Biophys. Acta 1136 (1992) 113-118
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 113-118
    • Voest, E.E.1    van Faassen, E.2    van Asbeck, B.S.3    Neijt, J.P.4    Marx, J.J.5
  • 18
    • 0037078918 scopus 로고    scopus 로고
    • Differential protection by nitroxides and hydroxylamines to radiation-induced and metal ion-catalyzed oxidative damage
    • Xavier S., Yamada K., Samuni A.M., Samuni A., DeGraff W., Krishna M.C., and Mitchell J.B. Differential protection by nitroxides and hydroxylamines to radiation-induced and metal ion-catalyzed oxidative damage. Biochim. Biophys. Acta 1573 (2002) 109-120
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 109-120
    • Xavier, S.1    Yamada, K.2    Samuni, A.M.3    Samuni, A.4    DeGraff, W.5    Krishna, M.C.6    Mitchell, J.B.7
  • 20
    • 0031962667 scopus 로고    scopus 로고
    • Both hydroxylamine and nitroxide protect cardiomyocytes from oxidative stress
    • Zhang R., Pinson A., and Samuni A. Both hydroxylamine and nitroxide protect cardiomyocytes from oxidative stress. Free Radic. Biol. Med. 24 (1998) 66-75
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 66-75
    • Zhang, R.1    Pinson, A.2    Samuni, A.3
  • 21
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman P.M., Muqit M.M., and Wood N.W. Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev., Neurosci. 7 (2006) 207-219
    • (2006) Nat. Rev., Neurosci. , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 22
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S., and Robinson B.H. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem. Sci. 25 (2000) 502-508
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 24
    • 33646684516 scopus 로고    scopus 로고
    • New insights into structure and function of mitochondria and their role in aging and disease
    • Lenaz G., Baracca A., Fato R., Genova M.L., and Solaini G. New insights into structure and function of mitochondria and their role in aging and disease. Antioxid. Redox Signal. 8 (2006) 417-437
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 417-437
    • Lenaz, G.1    Baracca, A.2    Fato, R.3    Genova, M.L.4    Solaini, G.5
  • 25
    • 33644953299 scopus 로고    scopus 로고
    • Calcium, mitochondria and oxidative stress in neuronal pathology. Novel aspects of an enduring theme
    • Chinopoulos C., and Adam-Vizi V. Calcium, mitochondria and oxidative stress in neuronal pathology. Novel aspects of an enduring theme. FEBS J. 273 (2006) 433-450
    • (2006) FEBS J. , vol.273 , pp. 433-450
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 26
    • 0021961622 scopus 로고
    • Reduction of the spin-label TEMPONE by ubiquinol in the electron transport chain of intact rabbit spermatozoa
    • Chapman D.A., Killian G.J., Gelerinter E., and Jarrett M.T. Reduction of the spin-label TEMPONE by ubiquinol in the electron transport chain of intact rabbit spermatozoa. Biol. Reprod. 32 (1985) 884-893
    • (1985) Biol. Reprod. , vol.32 , pp. 884-893
    • Chapman, D.A.1    Killian, G.J.2    Gelerinter, E.3    Jarrett, M.T.4
  • 27
    • 0023707088 scopus 로고
    • Kinetics of enzyme-mediated reduction of lipid soluble nitroxide spin labels by living cells
    • Chen K., Morse II P.D., and Swartz H.M. Kinetics of enzyme-mediated reduction of lipid soluble nitroxide spin labels by living cells. Biochim. Biophys. Acta 943 (1988) 477-484
    • (1988) Biochim. Biophys. Acta , vol.943 , pp. 477-484
    • Chen, K.1    Morse II, P.D.2    Swartz, H.M.3
  • 28
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy M.P., and Smith R.A. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 629-656
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 30
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin M.L., Meier T., Smith R.A., and Murphy M.P. Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J. 17 (2003) 1972-1974
    • (2003) FASEB J. , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 32
    • 0343986284 scopus 로고    scopus 로고
    • Drug delivery to mitochondria: the key to mitochondrial medicine
    • Murphy M.P., and Smith R.A. Drug delivery to mitochondria: the key to mitochondrial medicine. Adv. Drug Deliv. Rev. 41 (2000) 235-250
    • (2000) Adv. Drug Deliv. Rev. , vol.41 , pp. 235-250
    • Murphy, M.P.1    Smith, R.A.2
  • 35
    • 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
  • 36
    • 0037025274 scopus 로고    scopus 로고
    • Selective targeting of synthetic antioxidants to mitochondria: towards a mitochondrial medicine for neurodegenerative diseases?
    • Dessolin J., Schuler M., Quinart A., De Giorgi F., Ghosez L., and Ichas F. Selective targeting of synthetic antioxidants to mitochondria: towards a mitochondrial medicine for neurodegenerative diseases?. Eur. J. Pharmacol. 447 (2002) 155-161
    • (2002) Eur. J. Pharmacol. , vol.447 , pp. 155-161
    • Dessolin, J.1    Schuler, M.2    Quinart, A.3    De Giorgi, F.4    Ghosez, L.5    Ichas, F.6
  • 38
    • 40949146971 scopus 로고
    • N-Oxyl-Derivate des 2,2,6,6- Tetramethylpiperidins und deren Herstellung
    • Kaufhold M., Bueschken W., and Bickert P. N-Oxyl-Derivate des 2,2,6,6- Tetramethylpiperidins und deren Herstellung. German patent application DE924219471 (1993) 6
    • (1993) German patent application , vol.DE924219471 , pp. 6
    • Kaufhold, M.1    Bueschken, W.2    Bickert, P.3
  • 40
    • 0021826632 scopus 로고
    • Factors affecting nitroxide reduction in ascorbate solution and tissue homogenates
    • Couet W.R., Brasch R.C., Sosnovsky G., and Tozer T.N. Factors affecting nitroxide reduction in ascorbate solution and tissue homogenates. Magn. Reson. Imag. 3 (1985) 83-88
    • (1985) Magn. Reson. Imag. , vol.3 , pp. 83-88
    • Couet, W.R.1    Brasch, R.C.2    Sosnovsky, G.3    Tozer, T.N.4
  • 42
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A.G., Bardawill C.J., and David M.M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177 (1949) 751-766
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 43
    • 77957003097 scopus 로고
    • Preparation, properties, and condition for assay of mitochondria: slaughterhouse material, small-scale
    • Smith A.L. Preparation, properties, and condition for assay of mitochondria: slaughterhouse material, small-scale. Methods Enzymol. 10 (1967) 81-86
    • (1967) Methods Enzymol. , vol.10 , pp. 81-86
    • Smith, A.L.1
  • 44
    • 0028881842 scopus 로고
    • Structural analysis of NADH: ubiquinone oxidoreductase from bovine heart mitochondria
    • Walker J.E., Skehel J.M., and Buchanan S.K. Structural analysis of NADH: ubiquinone oxidoreductase from bovine heart mitochondria. Methods Enzymol. 260 (1995) 14-34
    • (1995) Methods Enzymol. , vol.260 , pp. 14-34
    • Walker, J.E.1    Skehel, J.M.2    Buchanan, S.K.3
  • 45
    • 0034630103 scopus 로고    scopus 로고
    • Genetic evidence for a multi- subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis
    • Hsu A.Y., Do T.Q., Lee P.T., and Clarke C.F. Genetic evidence for a multi- subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis. Biochim. Biophys. Acta 1484 (2000) 287-297
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 287-297
    • Hsu, A.Y.1    Do, T.Q.2    Lee, P.T.3    Clarke, C.F.4
  • 46
    • 0028800976 scopus 로고
    • Isolation of highly purified mitochondria from Saccharomyces cerevisiae
    • Glick B.S., and Pon L.A. Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods Enzymol. 260 (1995) 213-223
    • (1995) Methods Enzymol. , vol.260 , pp. 213-223
    • Glick, B.S.1    Pon, L.A.2
  • 49
    • 0026492717 scopus 로고
    • Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils
    • Lucas M., and Solano F. Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils. Anal. Biochem. 206 (1992) 273-277
    • (1992) Anal. Biochem. , vol.206 , pp. 273-277
    • Lucas, M.1    Solano, F.2
  • 50
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state
    • Kamo N., Muratsugu M., Hongoh R., and Kobatake Y. Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J. Membr. Biol. 49 (1979) 105-121
    • (1979) J. Membr. Biol. , vol.49 , pp. 105-121
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3    Kobatake, Y.4
  • 51
  • 52
    • 0022425351 scopus 로고
    • Thermodynamic control of electron flux through mitochondrial cytochrome bc1 complex
    • Brown G.C., and Brand M.D. Thermodynamic control of electron flux through mitochondrial cytochrome bc1 complex. Biochem. J. 225 (1985) 399-405
    • (1985) Biochem. J. , vol.225 , pp. 399-405
    • Brown, G.C.1    Brand, M.D.2
  • 53
    • 0033389582 scopus 로고    scopus 로고
    • Determination of ascorbate concentration in a raw leaf with electron spin resonance spectroscopy
    • Lin Y., Liu W., Ohno H., and Ogata T. Determination of ascorbate concentration in a raw leaf with electron spin resonance spectroscopy. Anal. Sci. 15 (1999) 973-977
    • (1999) Anal. Sci. , vol.15 , pp. 973-977
    • Lin, Y.1    Liu, W.2    Ohno, H.3    Ogata, T.4
  • 54
    • 4243650815 scopus 로고    scopus 로고
    • Evaluation of the potential for olestra to affect the availability of dietary phytochemicals
    • Cooper D.A., Webb D.R., and Peters J.C. Evaluation of the potential for olestra to affect the availability of dietary phytochemicals. J. Nutr. 127 (1997) 1699S-1709S
    • (1997) J. Nutr. , vol.127
    • Cooper, D.A.1    Webb, D.R.2    Peters, J.C.3
  • 56
    • 0011230350 scopus 로고
    • Surface localization of sites of reduction of nitroxide spin-labeled molecules in mitochondria
    • Quintanilha A.T., and Packer L. Surface localization of sites of reduction of nitroxide spin-labeled molecules in mitochondria. Proc. Natl. Acad. Sci. USA 74 (1977) 570-574
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 570-574
    • Quintanilha, A.T.1    Packer, L.2
  • 57
    • 0021758697 scopus 로고
    • Electron and proton transfers through quinones and cytochrome bc complexes
    • Rich P.R. Electron and proton transfers through quinones and cytochrome bc complexes. Biochim. Biophys. Acta 768 (1984) 53-79
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 53-79
    • Rich, P.R.1
  • 58
    • 0014961860 scopus 로고
    • One-electron reactions in biochemical systems as studied by pulse radiolysis. 3. Ubiquinone
    • Land E.J., and Swallow A.J. One-electron reactions in biochemical systems as studied by pulse radiolysis. 3. Ubiquinone. J. Biol. Chem. 245 (1970) 1890-1894
    • (1970) J. Biol. Chem. , vol.245 , pp. 1890-1894
    • Land, E.J.1    Swallow, A.J.2
  • 59
    • 1042278892 scopus 로고    scopus 로고
    • Antioxidant and prooxidant properties of mitochondrial Coenzyme Q
    • James A.M., Smith R.A., and Murphy M.P. Antioxidant and prooxidant properties of mitochondrial Coenzyme Q. Arch. Biochem. Biophys. 423 (2004) 47-56
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 47-56
    • James, A.M.1    Smith, R.A.2    Murphy, M.P.3
  • 64
    • 0023718724 scopus 로고
    • Oxidation of hydroxylamines to nitroxide spin labels in living cells
    • Chen K., and Swartz H.M. Oxidation of hydroxylamines to nitroxide spin labels in living cells. Biochim. Biophys. Acta 970 (1988) 270-277
    • (1988) Biochim. Biophys. Acta , vol.970 , pp. 270-277
    • Chen, K.1    Swartz, H.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.