메뉴 건너뛰기




Volumn 406, Issue 1, 2007, Pages 125-129

Succinate modulation of H2O2 release at NADH:ubiquinone oxidoreductase (Complex I) in brain mitochondria

Author keywords

Brain mitochondrion; Electron transfer; Hydrogen peroxide production; NADH:ubiquinone oxidoreductase (Complex I); Reactive oxygen species; Succinate

Indexed keywords

BRAIN; CELLS; ELECTRON TRANSITIONS; HYDROGEN PEROXIDE; OXIDATION;

EID: 34547850680     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070215     Document Type: Article
Times cited : (51)

References (23)
  • 1
    • 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. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 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
  • 4
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by Complex III of heart mitochondria
    • Turrens, J. F., Alexandre, A. and Lehninger, A. L. (1985) Ubisemiquinone is the electron donor for superoxide formation by Complex III of heart mitochondria. Arch. Biochem. Biophys. 237, 408-414
    • (1985) Arch. Biochem. Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 6
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas, E. and Davies, K. J. (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biol. Med. 29, 222-230
    • (2000) Free Radical Biol. Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 7
    • 0033963704 scopus 로고    scopus 로고
    • Oxidative stress and gene regulation
    • Allen, R. G. and Tresini, M. (2000) Oxidative stress and gene regulation. Free Radical Biol. Med. 28, 463-499
    • (2000) Free Radical Biol. Med , vol.28 , pp. 463-499
    • Allen, R.G.1    Tresini, M.2
  • 8
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens, J. F. and Boveris, A. (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191, 421-427
    • (1980) Biochem. J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 10
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu, Y., Fiskum, G. and Schubert, D. (2002) Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80, 780-787
    • (2002) J. Neurochem , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 11
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S. S., Skulachev, V. P. and Starkov, A. A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 12
    • 0034740585 scopus 로고    scopus 로고
    • m- dependent and independent production of reactive oxygen species by brain mitochondria
    • m- dependent and independent production of reactive oxygen species by brain mitochondria. J. Neurochem. 79, 266-277
    • (2001) J. Neurochem , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 13
    • 0142210179 scopus 로고    scopus 로고
    • Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria
    • Han, D., Canali, R., Rettori, D. and Kaplowitz, N. (2003) Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol. Pharmacol. 64, 1136-1144
    • (2003) Mol. Pharmacol , vol.64 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 16
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (Complex I) depends on the pH gradient across the mitochondrial inner membrane
    • Lambert, A. J. and Brand, M. D. (2004) Superoxide production by NADH:ubiquinone oxidoreductase (Complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382, 511-517
    • (2004) Biochem. J , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 17
    • 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. (2004) Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (Complex I). J. Biol. Chem. 279, 39414-39420
    • (2004) J. Biol. Chem , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 18
    • 0002456587 scopus 로고
    • α-Ketoglutarate dehydrogenase from pig heart
    • Sanadi, D. R. (1969) α-Ketoglutarate dehydrogenase from pig heart. Methods in Enzymol. 13, 52-55
    • (1969) Methods in Enzymol , vol.13 , pp. 52-55
    • Sanadi, D.R.1
  • 19
    • 0018363365 scopus 로고
    • The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex
    • McCormarck, J. G. and Denton, R. M. (1979) The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochem. J. 189, 533-544
    • (1979) Biochem. J , vol.189 , pp. 533-544
    • McCormarck, J.G.1    Denton, R.M.2
  • 21
    • 31444433077 scopus 로고    scopus 로고
    • Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase
    • Mason, M. G., Nicholls, P., Wilson, M. T. and Cooper, C. E. (2006) Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase. Proc. Natl. Acad. Sci. U.S.A. 103, 708-713
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 708-713
    • Mason, M.G.1    Nicholls, P.2    Wilson, M.T.3    Cooper, C.E.4
  • 22
    • 10044230387 scopus 로고    scopus 로고
    • On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
    • Antunes, F., Boveris, A. and Cadenas, E. (2004) On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide. Proc. Natl. Acad. Sci. U.S.A. 101, 16774-16779
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 16774-16779
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.