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Volumn 1777, Issue 7-8, 2008, Pages 689-695

Sites of generation of reactive oxygen species in homogenates of brain tissue determined with the use of respiratory substrates and inhibitors

Author keywords

Brain tissue; Mitochondria; Reactive oxygen species; Respiratory chain complex I; Respiratory chain complex III

Indexed keywords

DIGITONIN; FLAVINE MONONUCLEOTIDE; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXYGEN; REACTIVE OXYGEN METABOLITE; SUCCINIC ACID; SUPEROXIDE;

EID: 50949088772     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.05.010     Document Type: Article
Times cited : (74)

References (37)
  • 1
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: where are we now?
    • Halliwell B. Oxidative stress and neurodegeneration: where are we now?. J. Neurochem. 97 (2006) 1634-1658
    • (2006) J. Neurochem. , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 2
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R.S., Nemoto S., and Finkel T. Mitochondria, oxidants, and aging. Cell 120 (2005) 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 3
    • 0028177211 scopus 로고
    • -{radical dot} in the production of HO.: in vitro and in vivo
    • -{radical dot} in the production of HO.: in vitro and in vivo. Free Radic. Biol. Med. 16 (1994) 29-33
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 29-33
    • Liochev, S.I.1    Fridovich, I.2
  • 5
    • 0022555845 scopus 로고
    • Reactive oxygen intermediates in biochemistry
    • Naqui A., Chance B., and Cadenas E. Reactive oxygen intermediates in biochemistry. Annu. Rev. Biochem. 55 (1986) 137-166
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 137-166
    • Naqui, A.1    Chance, B.2    Cadenas, E.3
  • 6
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • Wood P.M. The potential diagram for oxygen at pH 7. Biochem. J. 253 (1988) 287-289
    • (1988) Biochem. J. , vol.253 , pp. 287-289
    • Wood, P.M.1
  • 7
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y., Fiskum G., and Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80 (2002) 780-787
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 8
    • 1042301416 scopus 로고    scopus 로고
    • Characterization of superoxide-producing sites in isolated brain mitochondria
    • Kudin A.P., Bimpong-Buta N.Y., Vielhaber S., Elger C.E., and Kunz W.S. Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem. 279 (2004) 4127-4135
    • (2004) J. Biol. Chem. , vol.279 , pp. 4127-4135
    • Kudin, A.P.1    Bimpong-Buta, N.Y.2    Vielhaber, S.3    Elger, C.E.4    Kunz, W.S.5
  • 9
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova T.V., and Reynolds I.J. DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 79 (2001) 266-277
    • (2001) J. Neurochem. , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 10
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • Genova M.L., Ventura B., Giuliano G., Bovina C., Formiggini G., Parenti Castelli G., and Lenaz G. The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2. FEBS Lett. 505 (2001) 364-368
    • (2001) FEBS Lett. , vol.505 , pp. 364-368
    • Genova, M.L.1    Ventura, B.2    Giuliano, G.3    Bovina, C.4    Formiggini, G.5    Parenti Castelli, G.6    Lenaz, G.7
  • 11
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Lambert A.J., and Brand M.D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279 (2004) 39414-39420
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 12
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A., Cadenas E., and Stoppani A.O. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156 (1976) 435-444
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 13
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J., Buckingham J.A., Roebuck S.J., and Brand M.D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277 (2002) 44784-44790
    • (2002) J. Biol. Chem. , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 14
    • 18044391656 scopus 로고    scopus 로고
    • Characterization of superoxide production sites in isolated rat brain and skeletal muscle mitochondria
    • Kudin A.P., Debska-Vielhaber G., and Kunz W.S. Characterization of superoxide production sites in isolated rat brain and skeletal muscle mitochondria. Biomed. Pharmacother. 59 (2005) 163-168
    • (2005) Biomed. Pharmacother. , vol.59 , pp. 163-168
    • Kudin, A.P.1    Debska-Vielhaber, G.2    Kunz, W.S.3
  • 17
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • Tretter L., and Adam-Vizi V. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J. Neurosci. 24 (2004) 7771-7778
    • (2004) J. Neurosci. , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 18
    • 25644452043 scopus 로고    scopus 로고
    • Novel multifunctional neuroprotective iron chelator-monoamine oxidase inhibitor drugs for neurodegenerative diseases. In vivo selective brain monoamine oxidase inhibition and prevention of MPTP-induced striatal dopamine depletion
    • Gal S., Zheng H., Fridkin M., and Youdim M.B. Novel multifunctional neuroprotective iron chelator-monoamine oxidase inhibitor drugs for neurodegenerative diseases. In vivo selective brain monoamine oxidase inhibition and prevention of MPTP-induced striatal dopamine depletion. J. Neurochem. 95 (2005) 79-88
    • (2005) J. Neurochem. , vol.95 , pp. 79-88
    • Gal, S.1    Zheng, H.2    Fridkin, M.3    Youdim, M.B.4
  • 19
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause K.H. Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn. J. Infect. Dis. 57 (2004) S28-S29
    • (2004) Jpn. J. Infect. Dis. , vol.57
    • Krause, K.H.1
  • 21
    • 10444229539 scopus 로고    scopus 로고
    • Role of cytochrome P450 in chemical toxicity and oxidative stress: studies with CYP2E1
    • Gonzales F.J. Role of cytochrome P450 in chemical toxicity and oxidative stress: studies with CYP2E1. Mutat. Res. 569 (2005) 101-110
    • (2005) Mutat. Res. , vol.569 , pp. 101-110
    • Gonzales, F.J.1
  • 22
    • 0031722906 scopus 로고    scopus 로고
    • Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species
    • Spencer J.P., Jenner P., Daniel S.E., Lees A.J., Marsden D.C., and Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71 (1998) 2112-2122
    • (1998) J. Neurochem. , vol.71 , pp. 2112-2122
    • Spencer, J.P.1    Jenner, P.2    Daniel, S.E.3    Lees, A.J.4    Marsden, D.C.5    Halliwell, B.6
  • 23
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 24
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology
    • Forman H.J., and Azzi A. On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J. 11 (1997) 374-375
    • (1997) FASEB J. , vol.11 , pp. 374-375
    • Forman, H.J.1    Azzi, A.2
  • 25
    • 13844262622 scopus 로고    scopus 로고
    • Intracellular generation of reactive oxygen species by mitochondria
    • Nohl H., Gille L., and Staniek K. Intracellular generation of reactive oxygen species by mitochondria. Biochem. Pharmacol. 69 (2005) 719-723
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 719-723
    • Nohl, H.1    Gille, L.2    Staniek, K.3
  • 26
    • 2342573463 scopus 로고    scopus 로고
    • The mystery of reactive oxygen species derived from cell respiration
    • Nohl H., Gille L., and Staniek K. The mystery of reactive oxygen species derived from cell respiration. Acta Biochim. Pol. 51 (2004) 223-229
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 223-229
    • Nohl, H.1    Gille, L.2    Staniek, K.3
  • 27
    • 0346158357 scopus 로고    scopus 로고
    • Cell respiration and formation of reactive oxygen species: facts and artefacts
    • Nohl H., Kozlov A.V., Gille L., and Staniek K. Cell respiration and formation of reactive oxygen species: facts and artefacts. Biochem. Soc. Trans. 31 (2003) 1308-1311
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1308-1311
    • Nohl, H.1    Kozlov, A.V.2    Gille, L.3    Staniek, K.4
  • 29
    • 44949185670 scopus 로고    scopus 로고
    • Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells
    • Kuznetsov A.V., Veksler V., Gellerich F.N., Saks V., Margreiter R., and Kunz W.S. Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells. Nat. Protoc. 3 (2008) 965-976
    • (2008) Nat. Protoc. , vol.3 , pp. 965-976
    • Kuznetsov, A.V.1    Veksler, V.2    Gellerich, F.N.3    Saks, V.4    Margreiter, R.5    Kunz, W.S.6
  • 30
    • 0024548927 scopus 로고
    • Generation of hydrogen peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia
    • Cino M., and Del Maestro R.F. Generation of hydrogen peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia. Arch. Biochem. Biophys. 269 (1989) 623-638
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 623-638
    • Cino, M.1    Del Maestro, R.F.2
  • 31
    • 5344234747 scopus 로고    scopus 로고
    • Detection of hydrogen peroxide with Amplex Red: interference by NADH and reduced glutathione auto-oxidation
    • Votyakova T.V., and Reynolds I.J. Detection of hydrogen peroxide with Amplex Red: interference by NADH and reduced glutathione auto-oxidation. Arch. Biochem. Biophys. 431 (2004) 138-144
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 138-144
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 32
    • 0016689082 scopus 로고
    • The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes
    • Azzi A., Montecucco C., and Richter C. The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes. Biochem. Biophys. Res. Commun. 65 (1975) 597-603
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 597-603
    • Azzi, A.1    Montecucco, C.2    Richter, C.3
  • 33
    • 0034796353 scopus 로고    scopus 로고
    • Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment
    • Halliwell B. Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs Aging 18 (2001) 685-716
    • (2001) Drugs Aging , vol.18 , pp. 685-716
    • Halliwell, B.1
  • 34
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnareva Y., Murphy A.N., and Andreyev A. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368 (2002) 545-553
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 36
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 37
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul L., and Hirst J. The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 7607-7612
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.