메뉴 건너뛰기




Volumn 37, Issue 1, 2005, Pages 1-15

A possible site of superoxide generation in the complex I segment of rat heart mitochondria

Author keywords

Complex I; Fluorescence assay of hydrogen peroxide; Heart mitochondria; Iron sulfur cluster N2; Superoxide; Ubiquinone; Ubisemiquinone

Indexed keywords

ACID ANHYDRIDE; ADENOSINE TRIPHOSPHATE; DIPHENYLIODONIUM SALT; ETHOXYFORMIC ANHYDRIDE; GLUTAMIC ACID; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; IRON; MALIC ACID; PIERICIDIN A; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; SEMIQUINONE; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 20044384225     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10863-005-4117-y     Document Type: Article
Times cited : (114)

References (91)
  • 1
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondra in the short-lived rat than in the longevous pigeon
    • Barja, G., and Herrero, A. (1998). Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondra in the short-lived rat than in the longevous pigeon. J. Bioenerg. Biomembr. 30, 235-243.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 2
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos, A., and Moraes, C. T. (1999). Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274, 16188-16197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 6
    • 0031965168 scopus 로고    scopus 로고
    • Quantitative study of mitochondrial complex I in platelets of parkinsonian patients
    • Blandini, F., Nappi, G., and Greenamyre, J. T. (1998). Quantitative study of mitochondrial complex I in platelets of parkinsonian patients. Mov Disord 13, 11-15.
    • (1998) Mov Disord , vol.13 , pp. 11-15
    • Blandini, F.1    Nappi, G.2    Greenamyre, J.T.3
  • 7
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin snsensitive respiration
    • Boveris, A., and Cadenas, E. (1975). Mitochondrial production of superoxide anions and its relationship to the antimycin snsensitive respiration. FEBS Lett. 54, 311-314.
    • (1975) FEBS Lett. , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 8
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbalic oxygen
    • Boveris, A., and Chance, B. (1973). The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbalic oxygen. Biochem. J. 134, 707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 9
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris, A., Cadenas, E., and Stoppani, A. O. M. (1976). Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156, 435-444.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.M.3
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0038392255 scopus 로고    scopus 로고
    • Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?
    • Brandt, U., Kerscher, S., Drose, S., Zwicker, K., and Zickermann, V. (2003). Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism? FEBS Lett. 545, 9-17.
    • (2003) FEBS Lett. , vol.545 , pp. 9-17
    • Brandt, U.1    Kerscher, S.2    Drose, S.3    Zwicker, K.4    Zickermann, V.5
  • 13
    • 0024435190 scopus 로고
    • Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain
    • Burbaev, D. S., Moroz, I. A., Kotlyar, A. B., Sled, V. D., and Vinogradov, A. D. (1989). Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain. FEBS Lett. 254, 47-51.
    • (1989) FEBS Lett. , vol.254 , pp. 47-51
    • Burbaev, D.S.1    Moroz, I.A.2    Kotlyar, A.B.3    Sled, V.D.4    Vinogradov, A.D.5
  • 15
    • 0001920088 scopus 로고
    • Direct spectroscopic measurements of interaction of components of the respiratory chainwith ATP, ADP, phosphate, and uncoupling agents
    • Pergamon Press, Oxford, New York
    • Chance, B., and Hagihara, B. (1963). Direct spectroscopic measurements of interaction of components of the respiratory chainwith ATP, ADP, phosphate, and uncoupling agents. In Proceedings of the 5th International Congress of Biochemistry Vol. 5, Pergamon Press, Oxford, New York, pp. 3-13.
    • (1963) Proceedings of the 5th International Congress of Biochemistry , vol.5 , pp. 3-13
    • Chance, B.1    Hagihara, B.2
  • 17
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism
    • Crofts, A. R., Meinhardt, S. W., Jones, K. R., and Snozzi, M. (1983). The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism. Biochim. Biophys. Acta 723, 202-218.
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 19
    • 0028209931 scopus 로고
    • Natural variation in the potency and binding sites of mitochondrial quinone-like inhibitors
    • Degli Esposti, M., Crimi, M., and Ghelli, A. (1994). Natural variation in the potency and binding sites of mitochondrial quinone-like inhibitors. Biochem. Soc. Trans. 22, 209-213.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 209-213
    • Degli Esposti, M.1    Crimi, M.2    Ghelli, A.3
  • 20
    • 0040368216 scopus 로고    scopus 로고
    • Prospects for new restorative and neuroprotective treatmens in Parkinson's disease
    • Dunnett, S. B., and Bjorklund, A. (1999). Prospects for new restorative and neuroprotective treatmens in Parkinson's disease. Nature 359, A32-A39.
    • (1999) Nature , vol.359
    • Dunnett, S.B.1    Bjorklund, A.2
  • 21
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Struicdture-based mechanism of conversion
    • Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., and Pai, E. (2000). Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Struicdture-based mechanism of conversion. Proc. Natl. Acad. Sci. U.S.A. 97, 10723-10728.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Nishino, T.5    Pai, E.6
  • 23
    • 0347481386 scopus 로고    scopus 로고
    • Iron-sulfur cluster N2 of the Escherichia coli NADH: Ubiquinone oxidoreductase (complex I) is located on subunit Nuo B
    • Flemming, D., Schlitt, A., Spehr, V., Boishof, T., and Friedrich, T. (2003). Iron-sulfur cluster N2 of the Escherichia coli NADH: Ubiquinone oxidoreductase (complex I) is located on subunit Nuo B. J. Biol. Chem. 276, 47602-47609.
    • (2003) J. Biol. Chem. , vol.276 , pp. 47602-47609
    • Flemming, D.1    Schlitt, A.2    Spehr, V.3    Boishof, T.4    Friedrich, T.5
  • 24
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury, C., Mignotte, B., and Vayssiere, J. (2002). Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84, 131-141.
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssiere, J.3
  • 25
    • 0027976420 scopus 로고
    • Two binding sites of inhibitors in NAADH ubiquinone oxidoreductase (complex I): Relationship of one site with the ubiquinone-binding site of bacterial glucose ubiquinone oxidoreductase
    • Friedrich, T., van Heek, P., Ohnishi, T., Forche, E., Kunze, B., Jansen, R., Trowitzsche-Kienast, W., Hofle, G., Reichenbach, H., and Weiss, H. (1994). Two binding sites of inhibitors in NAADH ubiquinone oxidoreductase (complex I): Relationship of one site with the ubiquinone-binding site of bacterial glucose ubiquinone oxidoreductase. Eur. J. Biochem. 2196.
    • (1994) Eur. J. Biochem. , pp. 2196
    • Friedrich, T.1    Van Heek, P.2    Ohnishi, T.3    Forche, E.4    Kunze, B.5    Jansen, R.6    Trowitzsche-Kienast, W.7    Hofle, G.8    Reichenbach, H.9    Weiss, H.10
  • 26
    • 0035501243 scopus 로고    scopus 로고
    • Role of long chain fatty acids and carnitine in mitochondrial membrane permeability transition
    • Furuno, T., Kanno, T., Arita, K., Asami, M., Utsumi, T., Doi, Y., Inoue, M., and Utsumi, K. (2001). Role of long chain fatty acids and carnitine in mitochondrial membrane permeability transition. Biochem. Pharmacol. 62, 1037-1046.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 1037-1046
    • Furuno, T.1    Kanno, T.2    Arita, K.3    Asami, M.4    Utsumi, T.5    Doi, Y.6    Inoue, M.7    Utsumi, K.8
  • 27
    • 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, C. G., and Lenaz, G. (2001). 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, 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, C.G.6    Lenaz, G.7
  • 28
    • 0028486222 scopus 로고
    • Idebenone. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic use in age-related cognitive disorders
    • Gillis, J. C., Benfield, P., and McTavish, D. (1994). Idebenone. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic use in age-related cognitive disorders. Drugs Aging 5, 133-152.
    • (1994) Drugs Aging , vol.5 , pp. 133-152
    • Gillis, J.C.1    Benfield, P.2    McTavish, D.3
  • 29
    • 0030969014 scopus 로고    scopus 로고
    • Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition
    • Grivennikova, V. G., Maklashina, E. O., Gavrikova, E. V., and Vinogradov, A. D. (1997). Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition. Biochim. Biophys. Acta 1319, 223-232.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 223-232
    • Grivennikova, V.G.1    Maklashina, E.O.2    Gavrikova, E.V.3    Vinogradov, A.D.4
  • 30
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross, A., Yin, X. M., Wang, K., Wei, M. C., Jockel, J., Milliman, C., Erdjument-Bromage, H., Tempst, P., and Korsmeyer, S. J. (1999). Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 274, 1156-1163.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 31
    • 0026754574 scopus 로고
    • Reactive oxygen species in the centrl nervous system
    • Halliwell, B. (1992). Reactive oxygen species in the centrl nervous system. J. Neurochem. 59, 1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 32
    • 0034467677 scopus 로고    scopus 로고
    • Localization of site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria
    • Herrero, A., and Barja, G. (2000). Localization of site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria. J. Bioenerg. Biomembr. 32, 609-615.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 609-615
    • Herrero, A.1    Barja, G.2
  • 35
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulfur centres in site I of mitochondria
    • Ingledew, W. J., and Ohnishi, T. (1980). An analysis of some thermodynamic properties of iron-sulfur centres in site I of mitochondria. Biochem. J. 186, 111-117.
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 36
    • 0042767578 scopus 로고    scopus 로고
    • Characterization of inhibitor binding sites of mitochondrial complex I using fluorescent inhibitor
    • Ino, T., Nishioka, T., and Miyoshi, H. (2003). Characterization of inhibitor binding sites of mitochondrial complex I using fluorescent inhibitor. Biochim. Biophys. Acta 1605, 15-20.
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 15-20
    • Ino, T.1    Nishioka, T.2    Miyoshi, H.3
  • 37
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the E. coli fumarate reductase respiratory complex
    • Iverson, T., Luna-Chavez, C., Cecchini, G., and Rees, D. C. (1999). Structure of the E. coli fumarate reductase respiratory complex. Science 284, 1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 38
    • 0141684565 scopus 로고    scopus 로고
    • NADH-ubiquinone oxidoreductase: Substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide
    • Johnson, J. E., Jr., Choksi, K., and Widger, W. R. (2003). NADH-ubiquinone oxidoreductase: Substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide. Mitochondrion 3, 97-110.
    • (2003) Mitochondrion , vol.3 , pp. 97-110
    • Johnson Jr., J.E.1    Choksi, K.2    Widger, W.R.3
  • 39
    • 0025072729 scopus 로고
    • Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase
    • Kotlyar, A. B., and Vinogradov, A. D. (1990). Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta 1019, 151-158.
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 151-158
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 40
    • 1042301416 scopus 로고    scopus 로고
    • Characterization of superoxide-producing sites in isolated brain mitochondria
    • Kudin, A. P., Bimpong-Buta, N. Y.-B., Vielhaber, S., Elger, C. E., and Kunz, W. S. (2004). Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem. 279, 4127-4135.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4127-4135
    • Kudin, A.P.1    Bimpong-Buta, N.Y.-B.2    Vielhaber, S.3    Elger, C.E.4    Kunz, W.S.5
  • 41
    • 0036903625 scopus 로고    scopus 로고
    • Complex-I mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnaeva, Y., Murrhy, A. N., and Andreyev, A. (2002). Complex-I mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368, 545-553.
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnaeva, Y.1    Murrhy, A.N.2    Andreyev, A.3
  • 42
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitocondrial NADH:ubiquinone oxidoreductase (compolex I)
    • Lambert, A. J., and Brant, M. D. (2004). Inhibitors of the quinone-binding site allow rapid superoxide production from mitocondrial NADH:ubiquinone oxidoreductase (compolex I). J. Biol. Chem. 279, 39414-39420.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brant, M.D.2
  • 43
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
    • Lancaster, C. R. D., Kröger, A., Auer, M., and Michel, H. (1999). Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution. Nature 402, 377-385.
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.D.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 45
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport
    • Liu, Y., Fiskum, G., and Schubert, D. (2002). Generation of reactive oxygen species by the mitochondrial electron transport. J. Neurochem. 80, 780-787.
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 46
    • 50549169010 scopus 로고
    • Succinate-linked diphosphopyridine nucleotide reduction in submitochondrial particles
    • Löw, H., and Vallin, I. (1963). Succinate-linked diphosphopyridine nucleotide reduction in submitochondrial particles. Biochim. Biophys. Acta 69, 361-374.
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 361-374
    • Löw, H.1    Vallin, I.2
  • 47
    • 0028558576 scopus 로고
    • The development of mitochondrial medicine
    • Luft, R. (1994). The development of mitochondrial medicine. Proc. Natl. Acad. Sci. USA 91, 8731-8738.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8731-8738
    • Luft, R.1
  • 49
    • 0142106477 scopus 로고    scopus 로고
    • Active/deactice transition of respiratory complex I in bacteria, fungi, and animals
    • Maklashina, E., Kotylyar, A. B., and Cecchini, G. (2003). Active/deactice transition of respiratory complex I in bacteria, fungi, and animals. Biochim. Biophys. Acta 1606, 95-103.
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 95-103
    • Maklashina, E.1    Kotylyar, A.B.2    Cecchini, G.3
  • 50
    • 0037015692 scopus 로고    scopus 로고
    • Effect of anoxia/reperfusion on the reversible active/de-active transition of NADH-ubiquinone oxidoreductase (complex I) in rat heart
    • Maklashina, E., Sher, Y., Zhou, H.-Z., Gray, M. O., Karliner, J. S., and Cecchini, G. (2002). Effect of anoxia/reperfusion on the reversible active/de-active transition of NADH-ubiquinone oxidoreductase (complex I) in rat heart. Biochim. Biophys. Acta 1556, 6-12.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 6-12
    • Maklashina, E.1    Sher, Y.2    Zhou, H.-Z.3    Gray, M.O.4    Karliner, J.S.5    Cecchini, G.6
  • 51
    • 2542421934 scopus 로고    scopus 로고
    • Substrate-induced conformational change in bacterial complex I
    • Mamedova, A. A., Holt, P. J., Carroll, J., and Sazanov, L. A. (2004). Substrate-induced conformational change in bacterial complex I. J. Biol. Chem. 279, 23830-23836.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23830-23836
    • Mamedova, A.A.1    Holt, P.J.2    Carroll, J.3    Sazanov, L.A.4
  • 52
    • 0032559799 scopus 로고    scopus 로고
    • The caspase-3 precursor has a cytosolic and mitochondrial distribution: Implications for apoptotic signaling
    • Mancini, M., Nicholson, D., Roy, S., Thornberry, N., Peterson, E., Casciola-Rosen, L., and Rosen, A. ( 1998). The caspase-3 precursor has a cytosolic and mitochondrial distribution: Implications for apoptotic signaling. J. Cell Biol. 140, 1485-1495.
    • (1998) J. Cell Biol. , vol.140 , pp. 1485-1495
    • Mancini, M.1    Nicholson, D.2    Roy, S.3    Thornberry, N.4    Peterson, E.5    Casciola-Rosen, L.6    Rosen, A.7
  • 54
    • 0018401677 scopus 로고
    • Isolation of mitochondria with emphasis on heart mitochondria from small amounts of tissue
    • Mela, L., and Seitz, S. (1979). Isolation of mitochondria with emphasis on heart mitochondria from small amounts of tissue. Methods Enzymol. 55, 39-46.
    • (1979) Methods Enzymol. , vol.55 , pp. 39-46
    • Mela, L.1    Seitz, S.2
  • 55
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell, P. (1975). The protonmotive Q cycle: a general formulation. FEBS Lett. 59, 137-139.
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 56
    • 0346788896 scopus 로고    scopus 로고
    • Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling
    • Miwa, S., and Brand, M. D. (2003). Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling. Biochem. Soc. Trans. 31, 1300-1301.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1300-1301
    • Miwa, S.1    Brand, M.D.2
  • 57
    • 0037070166 scopus 로고    scopus 로고
    • Quinones in long-lived clk-1 mutants of Caenorhabditis elegans
    • Miyadera, H., Kano, K., Miyoshi, H., Ishii, N., Hekimi, S., and Kita, K. (2002). Quinones in long-lived clk-1 mutants of Caenorhabditis elegans. FEBS Lett. 512, 33-37.
    • (2002) FEBS Lett. , vol.512 , pp. 33-37
    • Miyadera, H.1    Kano, K.2    Miyoshi, H.3    Ishii, N.4    Hekimi, S.5    Kita, K.6
  • 58
    • 0023186383 scopus 로고
    • Effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and 1-methyl-4-phenylpyridinium ion on activities of the enzymes in the electron transport system in mouse brain
    • Mizuno, Y., Sone, N., and Saitoh, T. (1987). Effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and 1-methyl-4-phenylpyridinium ion on activities of the enzymes in the electron transport system in mouse brain. J. Neurochem. 48, 1787-1793.
    • (1987) J. Neurochem. , vol.48 , pp. 1787-1793
    • Mizuno, Y.1    Sone, N.2    Saitoh, T.3
  • 60
    • 0034442070 scopus 로고    scopus 로고
    • The nature mechanism of superoxide productionby the electron transpot chain: Its relevance to aging
    • Muller, F. (2000). The nature mechanism of superoxide productionby the electron transpot chain: Its relevance to aging. J. Am. Aging Assoc. 23, 227-253.
    • (2000) J. Am. Aging Assoc. , vol.23 , pp. 227-253
    • Muller, F.1
  • 63
    • 0002075231 scopus 로고
    • Structure of the succinate-ubiquinone oxidoreductase (complex II)
    • (Lee, C. P., ed.), Academic Press, New York
    • Ohnishi, T. (1987). Structure of the succinate-ubiquinone oxidoreductase (complex II). In Current Topics in Bioenergetics (Lee, C. P., ed.), Vol. 15, Academic Press, New York, pp. 37-65.
    • (1987) Current Topics in Bioenergetics , vol.15 , pp. 37-65
    • Ohnishi, T.1
  • 64
    • 0032490089 scopus 로고    scopus 로고
    • Iron sulfur clusters/semiquinones in complex I
    • Ohnishi, T. (1998). Iron sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta 1364, 186-206.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 65
    • 0018971809 scopus 로고
    • Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate-cytochrome c reductase complex
    • Ohnishi, T., and Trumpower, B. L. (1980). Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate-cytochrome c reductase complex. J. Biol. Chem. 255, 3278-3284.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3278-3284
    • Ohnishi, T.1    Trumpower, B.L.2
  • 66
    • 11844287666 scopus 로고    scopus 로고
    • Thermodynamic and EPR studies of slowly-relaxing SQ species in the isolated bovine heart complex I
    • Ohnishi, T., Johnson, J. E., Jr., Yano, T., LoBrutto, R., and Widger, W. R. (2005). Thermodynamic and EPR studies of slowly-relaxing SQ species in the isolated bovine heart complex I. FEBS Lett. 579, 500-506.
    • (2005) FEBS Lett. , vol.579 , pp. 500-506
    • Ohnishi, T.1    Johnson Jr., J.E.2    Yano, T.3    LoBrutto, R.4    Widger, W.R.5
  • 67
    • 0028102945 scopus 로고
    • Effect of ethoxyformic anyhydride on the Rieske iron-sulfur protein of bovine heart ubiquinol: Cytochrome c oxidoreductase
    • Ohnishi, T., Meinhardt, S. W., von Jagow, G., Yagi, T., and Hatefi, Y. ( 1994). Effect of ethoxyformic anyhydride on the Rieske iron-sulfur protein of bovine heart ubiquinol: Cytochrome c oxidoreductase. FEBS Lett. 353, 103-107.
    • (1994) FEBS Lett. , vol.353 , pp. 103-107
    • Ohnishi, T.1    Meinhardt, S.W.2    Von Jagow, G.3    Yagi, T.4    Hatefi, Y.5
  • 68
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
    • Okun, J. G., Lummen, P., and Brandt, U. (1999). Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase). J. Biol. Chem. 274, 2625-2630.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 69
    • 33748638376 scopus 로고    scopus 로고
    • The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solution in contact with oxygen
    • Petlicki, J., and van de Ven, T. G. M. (1998). The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solution in contact with oxygen. J. Chem. Soc. Faraday Trans. 94, 2763-2767.
    • (1998) J. Chem. Soc. Faraday Trans. , vol.94 , pp. 2763-2767
    • Petlicki, J.1    Van De Ven, T.G.M.2
  • 70
    • 85023405438 scopus 로고
    • Structure of NADH-ubiquinone reductase (Complex I)
    • Ragan, C. I. (1987). Structure of NADH-ubiquinone reductase (Complex I). Curr. Top. Bioenerg. 15, 1-36.
    • (1987) Curr. Top. Bioenerg. , vol.15 , pp. 1-36
    • Ragan, C.I.1
  • 71
    • 20044362862 scopus 로고
    • Iron-sulphur proteins of mitochondrial NADH-ubiquinone reductase (complex I)
    • (Matsubara, H., et al., eds.), Japan Scientific Socities Press, Tokyo
    • Ragan, C. I., Ohnishi, T., and Hatefi, Y. (1986). Iron-sulphur proteins of mitochondrial NADH-ubiquinone reductase (complex I). In Iron-Sulfur Protein Research (Matsubara, H., et al., eds.), Japan Scientific Socities Press, Tokyo, pp. 220-231.
    • (1986) Iron-Sulfur Protein Research , pp. 220-231
    • Ragan, C.I.1    Ohnishi, T.2    Hatefi, Y.3
  • 72
    • 0027104639 scopus 로고
    • Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A and MPP+
    • Ramsay, R. R., and Singer, T. P. (1992). Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A and MPP+. Biochem. Biophys. Res. Commun. 189, 47-52.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 47-52
    • Ramsay, R.R.1    Singer, T.P.2
  • 73
    • 0032490099 scopus 로고    scopus 로고
    • Human complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect
    • Robinson, B. H. (1998). Human complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect. Biochim. Biophys. Acta 1364, 271-286.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 271-286
    • Robinson, B.H.1
  • 75
    • 0032490091 scopus 로고    scopus 로고
    • Human complex i defects in neurodegenerative diseases
    • Schapira, A. H. V. (1998). Human complex i defects in neurodegenerative diseases. Biochim. Biophys. Acta 1364, 261-270.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 261-270
    • Schapira, A.H.V.1
  • 76
    • 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. (1994). Thermodynamic analysis of flavin in mitochondrial NADH-ubiquinone oxidoreductase (complex I). Biochemistry 33, 10069-10075.
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 77
    • 0142195820 scopus 로고    scopus 로고
    • Superoxide anion generation by the cytochrome bc1 complex
    • Sun, J., and Trumpower, B. L. (2003). Superoxide anion generation by the cytochrome bc1 complex. Arch. Biochem. Biophys. 419, 198-206.
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 198-206
    • Sun, J.1    Trumpower, B.L.2
  • 78
    • 0018393931 scopus 로고
    • NADH and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation
    • Takeshige, K., and Minakami, S. (1979). NADH and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J. 180, 129-135.
    • (1979) Biochem. J. , vol.180 , pp. 129-135
    • Takeshige, K.1    Minakami, S.2
  • 79
    • 0346094388 scopus 로고    scopus 로고
    • Production of endogenous matrix superoxide from mitochondria complex K leads to activation of uncoupling protein 3
    • Talbot, D. A., Lambert, A. J., and Brand, M. D. (2004). Production of endogenous matrix superoxide from mitochondria complex K leads to activation of uncoupling protein 3. FEBS Lett. 556, 111-115.
    • (2004) FEBS Lett. , vol.556 , pp. 111-115
    • Talbot, D.A.1    Lambert, A.J.2    Brand, M.D.3
  • 82
    • 0019083215 scopus 로고
    • Generation of superoxide anion by NADH dehydrogenase of bovine heart mitochondria
    • Turrens, J. F., and Boveris, A. (1980). Generation of superoxide anion by 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
  • 83
    • 0033970827 scopus 로고    scopus 로고
    • The D-loop structure of human mtDNA is destabilized directly by 1-methyl-4-phenylpyridinium ion (MPP+), a parkinsonism-causing toxin
    • Umeda, S., Muta, T., and Ohsato, T. (2000). The D-loop structure of human mtDNA is destabilized directly by 1-methyl-4-phenylpyridinium ion (MPP+), a parkinsonism-causing toxin. Eur. J. Biochem. 267, 200-206.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 200-206
    • Umeda, S.1    Muta, T.2    Ohsato, T.3
  • 84
    • 0021526009 scopus 로고
    • Inhibition of mitochondrial NADH: Ubiquinone oxidoreductase by ethoxyformic anhydride
    • Vik, S. B., and Hatefi, Y. (1984). Inhibition of mitochondrial NADH: Ubiquinone oxidoreductase by ethoxyformic anhydride. Biochem. Int. 9, 547-555.
    • (1984) Biochem. Int. , vol.9 , pp. 547-555
    • Vik, S.B.1    Hatefi, Y.2
  • 85
    • 0032490104 scopus 로고    scopus 로고
    • Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition
    • Vinogradov, A. (1998). Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta 1364, 169-185.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 169-185
    • Vinogradov, A.1
  • 88
    • 13444259531 scopus 로고    scopus 로고
    • Nf) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I
    • Nf) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I. Biochemistry, 44, 1744-1754.
    • (2005) Biochemistry , vol.44 , pp. 1744-1754
    • Yano, T.1    Dunham, W.R.2    Ohnishi, T.3
  • 89
    • 0037844859 scopus 로고    scopus 로고
    • Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit od the proton-translocating NADH-ubiquinone oxidoeductase from paracoccus denitrificans
    • Yano, T., Sklar, J., Nakamaru-Ogiso, E., Takahashi, Y., Yagi, T., and Ohnishi, T. (2003). Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit od the proton-translocating NADH-ubiquinone oxidoeductase from paracoccus denitrificans. J. Biol. Chem. 278, 15514-15522.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15514-15522
    • Yano, T.1    Sklar, J.2    Nakamaru-Ogiso, E.3    Takahashi, Y.4    Yagi, T.5    Ohnishi, T.6
  • 91
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • Zhang, L., Yu, L., and Yu, C.-A. (1998). Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273, 33972-33976.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.-A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.