메뉴 건너뛰기




Volumn 46, Issue 11, 2012, Pages 1313-1326

Susceptibility of mitochondrial electron-transport complexes to oxidative damage. Focus on cytochrome c oxidase

Author keywords

Cardiolipin; Complex I; Complex III; Complex IV; Oxygen species; Reactive

Indexed keywords

CARDIOLIPIN; CYTOCHROME C; CYTOCHROME C OXIDASE; MEMBRANE PROTEIN; PEROXYNITRITE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 84867534243     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2012.717273     Document Type: Review
Times cited : (147)

References (140)
  • 1
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF, Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 1980; 191: 421-427.
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 2
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, Lehninger AL. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 1985; 237: 408-414.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 3
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 4
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992; 257: 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 5
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 2007; 87: 315-424.
    • (2007) Physiol Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 6
    • 0031021944 scopus 로고    scopus 로고
    • Mass spectrometric quantifi cation of markers for protein oxidation by tyrosyl radical, cooper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques
    • Leeuwenburgh C, Rasmussen JE, Hsu FF, Mueller DM, Pennathur S, Heinecke JW. Mass spectrometric quantifi cation of markers for protein oxidation by tyrosyl radical, cooper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques. J Biol Chem 1997; 272: 3520-3526.
    • (1997) J Biol Chem , vol.272 , pp. 3520-3526
    • Leeuwenburgh, C.1    Rasmussen, J.E.2    Hsu, F.F.3    Mueller, D.M.4    Pennathur, S.5    Heinecke, J.W.6
  • 7
    • 0029917194 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease
    • Hattori N, Uchida K, Tanaka M, Stadtman ER, Mizuno Y. Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc Natl Acad Sci USA 1996; 93: 2696-2701.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2696-2701
    • Hattori, N.1    Uchida, K.2    Tanaka, M.3    Stadtman, E.R.4    Mizuno, Y.5
  • 8
    • 0024370492 scopus 로고
    • Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy
    • Murphy ME, Kherer JP. Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy. Biochem J 1989; 260: 359-364.
    • (1989) Biochem J , vol.260 , pp. 359-364
    • Murphy, M.E.1    Kherer, J.P.2
  • 10
    • 0002105437 scopus 로고
    • Mitochondrial DNA mutations and bioenergetic defects in aging and degenerative diseases
    • In: Rosenberg RN, Prusiner SB, DiMauro S, Barchi RL (eds). Boston: Butterworth-Heinemann
    • Wallace DC. Mitochondrial DNA mutations and bioenergetic defects in aging and degenerative diseases. In: Rosenberg RN, Prusiner SB, DiMauro S, Barchi RL (eds). The molecular and genetic basis of neurological disease. Boston: Butterworth-Heinemann; 1993. pp. 237-269.
    • (1993) The Molecular and Genetic Basis of Neurological Disease , pp. 237-269
    • Wallace, D.C.1
  • 12
    • 0344925124 scopus 로고    scopus 로고
    • Ischemia-reperfusion injury in the aged heart: Role of mitochondria
    • Lesnefsky EJ, Hoppel CL. Ischemia-reperfusion injury in the aged heart: role of mitochondria. Arch Biochem Biophys 2003; 420: 287-297.
    • (2003) Arch Biochem Biophys , vol.420 , pp. 287-297
    • Lesnefsky, E.J.1    Hoppel, C.L.2
  • 14
    • 0019891622 scopus 로고
    • On the function of multiple subunits of cytochromec oxidase from higher eukaryotes
    • Kadenbach B, Merle P. On the function of multiple subunits of cytochromec oxidase from higher eukaryotes. FEBS Lett 1981; 135: 1-11.
    • (1981) FEBS Lett , vol.135 , pp. 1-11
    • Kadenbach, B.1    Merle, P.2
  • 15
    • 0026615057 scopus 로고
    • Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromec oxidase. Purifi cation, kinetics, proton pumping, and spectral analysis
    • Hosler JP, Fetter J, Tecklenburg MM, Espe M, Lerma C, Ferguson-Miller S. Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromec oxidase. Purifi cation, kinetics, proton pumping, and spectral analysis. J Biol Chem 1992; 267: 24264-24272.
    • (1992) J Biol Chem , vol.267 , pp. 24264-24272
    • Hosler, J.P.1    Fetter, J.2    Tecklenburg, M.M.3    Espe, M.4    Lerma, C.5    Ferguson-Miller, S.6
  • 16
    • 0035846967 scopus 로고    scopus 로고
    • Structure of cytochromec oxidase: A comparison of the bacterial and mitochondrial enzymes
    • Abramson J, Svensson-Ek M, Byrne B, Iwata S. Structure of cytochromec oxidase: a comparison of the bacterial and mitochondrial enzymes. Biochim Biophys Acta 2001; 1544: 1-9.
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 1-9
    • Abramson, J.1    Svensson-Ek, M.2    Byrne, B.3    Iwata, S.4
  • 17
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wildtype and EQ(I-286) mutant cytochromec oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M, Abramson J, Larsson G, Törnroth S, Brzezinski P, Iwata S. The X-ray crystal structures of wildtype and EQ(I-286) mutant cytochromec oxidases from Rhodobacter sphaeroides. J Mol Biol 2002; 321: 329-339.
    • (2002) J Mol Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 18
    • 0035849452 scopus 로고    scopus 로고
    • Role of the PR intermediate in the reaction of cytochromec oxidase with O 2
    • Morgan JE, Verchovsky MI, Palmer G, Wikström M. Role of the PR intermediate in the reaction of cytochromec oxidase with O 2. Biochemistry 2001; 40: 6882-6892.
    • (2001) Biochemistry , vol.40 , pp. 6882-6892
    • Morgan, J.E.1    Verchovsky, M.I.2    Palmer, G.3    Wikström, M.4
  • 19
    • 0035859920 scopus 로고    scopus 로고
    • Role of the K-channel in the pH-dependence of the reaction of cytochromec oxidase with hydrogen peroxide
    • Pecoraro C, Gennis RB, Vygodina TV, Konstantinov AA. Role of the K-channel in the pH-dependence of the reaction of cytochromec oxidase with hydrogen peroxide. Biochemistry 2001; 40: 9695-9708.
    • (2001) Biochemistry , vol.40 , pp. 9695-9708
    • Pecoraro, C.1    Gennis, R.B.2    Vygodina, T.V.3    Konstantinov, A.A.4
  • 20
    • 0028851789 scopus 로고
    • The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F
    • Fabian M, Palmer G. The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F. Biochemistry 1995; 34: 13802-13810.
    • (1995) Biochemistry , vol.34 , pp. 13802-13810
    • Fabian, M.1    Palmer, G.2
  • 22
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layer phospholipids of cytochromec oxidase using Triton X-100 delipidation
    • Robinson NC, Strey F, Talbert L. Investigation of the essential boundary layer phospholipids of cytochromec oxidase using Triton X-100 delipidation. Biochemistry 1980; 19: 3656-3661.
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 23
    • 0027252494 scopus 로고
    • Functional binding of cardiolipin to cytochromec oxidase
    • Robinson NC. Functional binding of cardiolipin to cytochromec oxidase. J Bioenerg Biomembr 1993; 25: 153-163.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 153-163
    • Robinson, N.C.1
  • 24
    • 84867559710 scopus 로고
    • The specifi city and affi nity of phospholipids for cytochromec oxidase
    • Robinson NC. The specifi city and affi nity of phospholipids for cytochromec oxidase. Biophys J 1982; 37: 65-66.
    • (1982) Biophys J , vol.37 , pp. 65-66
    • Robinson, N.C.1
  • 25
    • 0033539647 scopus 로고    scopus 로고
    • Phospholipase A(2) digestion of cardiolipin bound to bovine cytochromec oxidase alters both activity and quaternary structure
    • Sedlák E, Robinson NC. Phospholipase A(2) digestion of cardiolipin bound to bovine cytochromec oxidase alters both activity and quaternary structure. Biochemistry 1999; 38: 14966-14972.
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlák, E.1    Robinson, N.C.2
  • 26
    • 0020490631 scopus 로고
    • Cytochrome c oxidase binding of hydrogen peroxide
    • Bickar D, Bonaventura J, Bonaventura C. Cytochrome c oxidase binding of hydrogen peroxide. Biochemistry 1982; 24: 2661-2666.
    • (1982) Biochemistry , vol.24 , pp. 2661-2666
    • Bickar, D.1    Bonaventura, J.2    Bonaventura, C.3
  • 27
    • 0021380356 scopus 로고
    • Formation and reduction of a "peroxy" intermediate of cytochromec oxidase by hydrogen peroxide
    • Wrigglesworth JM. Formation and reduction of a "peroxy" intermediate of cytochromec oxidase by hydrogen peroxide. Biochem J 1984; 217: 715-719.
    • (1984) Biochem J , vol.217 , pp. 715-719
    • Wrigglesworth, J.M.1
  • 28
    • 0024515840 scopus 로고
    • Effect of pH on the spectrum of cytochromec oxidase hydrogen peroxide complex
    • Vygodina T, Konstantinov AA. Effect of pH on the spectrum of cytochromec oxidase hydrogen peroxide complex. Biochim Biophys Acta 1989; 973: 390-398.
    • (1989) Biochim Biophys Acta , vol.973 , pp. 390-398
    • Vygodina, T.1    Konstantinov, A.A.2
  • 29
    • 0025787382 scopus 로고
    • Reaction of hydrogen peroxide with the rapid form of resting cytochrome oxidase
    • Weng L, Baker GM. Reaction of hydrogen peroxide with the rapid form of resting cytochrome oxidase. Biochemistry 1991; 30: 5727-5733.
    • (1991) Biochemistry , vol.30 , pp. 5727-5733
    • Weng, L.1    Baker, G.M.2
  • 30
    • 1942506137 scopus 로고    scopus 로고
    • Modifi cation of nuclear-coded subunits of oxidized bovine heart cytochromec oxidase by hydrogen peroxide
    • Musatov A, Hebert E, Robinson NC. Modifi cation of nuclear-coded subunits of oxidized bovine heart cytochromec oxidase by hydrogen peroxide. Biochem Biophys Acta 2002; 12(Supplement): 96.
    • (2002) Biochem Biophys Acta , vol.12 , pp. 96
    • Musatov, A.1    Hebert, E.2    Robinson, N.C.3
  • 31
    • 0942290629 scopus 로고    scopus 로고
    • Specifi c modifi cation of two tryptophans within the nuclear-encoded subunits of bovine cytochromec oxidase by hydrogen peroxide
    • Musatov A, Hebert E, Carrol CA, Weintraub ST, Robinson NC. Specifi c modifi cation of two tryptophans within the nuclear-encoded subunits of bovine cytochromec oxidase by hydrogen peroxide. Biochemistry 2004; 43: 1003-1009.
    • (2004) Biochemistry , vol.43 , pp. 1003-1009
    • Musatov, A.1    Hebert, E.2    Carrol, C.A.3    Weintraub, S.T.4    Robinson, N.C.5
  • 32
    • 33846425366 scopus 로고    scopus 로고
    • Tryptophan 334 oxidation in bovine cytochromec oxidase subunit i involves free radical migration
    • Lemma-Gray P, Weintraub ST, Carroll CA, Musatov A, Robinson NC. Tryptophan 334 oxidation in bovine cytochromec oxidase subunit I involves free radical migration. FEBS Lett 2007; 581: 437-442.
    • (2007) FEBS Lett , vol.581 , pp. 437-442
    • Lemma-Gray, P.1    Weintraub, S.T.2    Carroll, C.A.3    Musatov, A.4    Robinson, N.C.5
  • 33
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modifi cation of tryptophan residues in cardiac mitochondrial proteins
    • Taylor SW, Fahy E, Murray J, Capaldi RA, Ghosh SS. Oxidative post-translational modifi cation of tryptophan residues in cardiac mitochondrial proteins. J Biol Chem 2003; 22: 19587-19590.
    • (2003) J Biol Chem , vol.22 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 34
    • 0033984710 scopus 로고    scopus 로고
    • The eff ect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochromec oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM. The eff ect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochromec oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett 2000; 466: 323-326.
    • (2000) FEBS Lett , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 35
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y, Marcillat O, Giulivi C, Ernster L, Davies KJA. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J Biol Chem 1990; 265: 16330-16336.
    • (1990) J Biol Chem , vol.265 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Kja, D.5
  • 36
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S, Palmer RM, Higgs EA. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 1991; 43: 109-142.
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 37
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton WK, Cooper CE, Knowles RG. Nitric oxide synthases: structure, function and inhibition. Biochem J 2001; 357: 593-615.
    • (2001) Biochem J , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 38
    • 0028134892 scopus 로고    scopus 로고
    • Nanomolar concetrations of nitric oxide reversibly inhibit synaptosomal cytochrome oxidase respiration by competing with oxygen at cytochrome oxidase
    • Brown GC, Cooper CE. Nanomolar concetrations of nitric oxide reversibly inhibit synaptosomal cytochrome oxidase respiration by competing with oxygen at cytochrome oxidase. FEBS Lett 2001; 356: 295-298.
    • (2001) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 41
    • 33845378793 scopus 로고
    • Reaction of superoxide with nitric oxide to form peroxynitrite in alkaline aqueous solution
    • Blough NV, Zafi riou OC. Reaction of superoxide with nitric oxide to form peroxynitrite in alkaline aqueous solution. Inorg Chem 1985; 24: 3502-3504.
    • (1985) Inorg Chem , vol.24 , pp. 3502-3504
    • Blough, N.V.1    Zafi Riou, O.C.2
  • 42
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex i due to peroxynitrite
    • Murray J, Taylor SW, Zhang B, Ghosh SS, Capaldi RA. Oxidative damage to mitochondrial complex I due to peroxynitrite. J Biol Chem 2003; 278: 37223-37230.
    • (2003) J Biol Chem , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 43
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown GC. Nitric oxide and mitochondrial respiration. Biochim Biophys Acta 1999; 1411: 351-369.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 44
    • 0029998238 scopus 로고    scopus 로고
    • Diff erent inhibitory actions of NO and peroxynitrite on mitochondrial electron transport
    • Cassina A, Radi R. Diff erent inhibitory actions of NO and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 1996; 328: 309-316.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 45
    • 0031571757 scopus 로고    scopus 로고
    • Calcium-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation
    • Gadelha FR, Thomson L, Fagian MM, Costa ADT, Radi R, Vercesi AE. Calcium-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation. Arch Biochem Biophys 1997; 345: 243-250.
    • (1997) Arch Biochem Biophys , vol.345 , pp. 243-250
    • Gadelha, F.R.1    Thomson, L.2    Fagian, M.M.3    Costa, A.D.T.4    Radi, R.5    Vercesi, A.E.6
  • 46
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Diff erential susceptibility of neurones and astrocytes in primary culture
    • Bolaños JP, Heales SJR, Land JM, Clark JB. Effect of peroxynitrite on the mitochondrial respiratory chain: diff erential susceptibility of neurones and astrocytes in primary culture. J Neurochem 1995; 64: 1965-1972.
    • (1995) J Neurochem , vol.64 , pp. 1965-1972
    • Bolaños, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 47
    • 0032553302 scopus 로고    scopus 로고
    • Interaction of peroxinitrite with mitochondrial cytochrome oxidase
    • Sharpe MA, Cooper CE. Interaction of peroxinitrite with mitochondrial cytochrome oxidase. J Biol Chem 1998; 273: 30961-30972.
    • (1998) J Biol Chem , vol.273 , pp. 30961-30972
    • Sharpe, M.A.1    Cooper, C.E.2
  • 48
  • 50
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • Radi R, Cassina A, Hodara R. Nitric oxide and peroxynitrite interactions with mitochondria. Biol Chem 2002; 383: 401-409.
    • (2002) Biol Chem , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 51
    • 0033544891 scopus 로고    scopus 로고
    • The peroxynitrite reductase activity of cytochromec oxidase involves a two-electron redox reaction at the heme a3-CuB site
    • Pearce LL, Pitt BR, Peterson J. The peroxynitrite reductase activity of cytochromec oxidase involves a two-electron redox reaction at the heme a3-CuB site. J Biol Chem 1999; 274: 35763-35767.
    • (1999) J Biol Chem , vol.274 , pp. 35763-35767
    • Pearce, L.L.1    Pitt, B.R.2    Peterson, J.3
  • 54
    • 0034235186 scopus 로고    scopus 로고
    • Oxidation of ubiquinol by peroxynitrite: Implications for protection of mitochondria against nitrosative damage
    • Schöpfer F, Riobó N, Carreras MC, Alvarez B, Radi R, Boveris A, et al. Oxidation of ubiquinol by peroxynitrite: implications for protection of mitochondria against nitrosative damage. Biochem J 2000; 349: 35-42.
    • (2000) Biochem J , vol.349 , pp. 35-42
    • Schöpfer, F.1    Riobó, N.2    Carreras, M.C.3    Alvarez, B.4    Radi, R.5    Boveris, A.6
  • 55
    • 46449083451 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegeneration: Cardiolipin, a critical target
    • Pope S, Land JM, Heales SJR. Oxidative stress and mitochondrial dysfunction in neurodegeneration: cardiolipin, a critical target? Biochem Biophys Acta 2008; 1777: 794-799.
    • (2008) Biochem Biophys Acta , vol.1777 , pp. 794-799
    • Pope, S.1    Land, J.M.2    Heales, S.J.R.3
  • 56
    • 50949108782 scopus 로고    scopus 로고
    • Cardiolipin as an oxidative target in cardiac mitochondria in the aged rat
    • Lesnefsky EJ, Hoppel CL. Cardiolipin as an oxidative target in cardiac mitochondria in the aged rat. Biochem Biophys Acta 2008; 1777: 1020-1027.
    • (2008) Biochem Biophys Acta , vol.1777 , pp. 1020-1027
    • Lesnefsky, E.J.1    Hoppel, C.L.2
  • 57
    • 24844480489 scopus 로고    scopus 로고
    • Removal of bound cardiolipin destabilizes the quaternary structure of bovine heart cytochromec oxidase
    • Sedlák E, Robinson NC. Removal of bound cardiolipin destabilizes the quaternary structure of bovine heart cytochromec oxidase. Biochim Biophys Acta (Suppl.) 2002; 12: 119.
    • (2002) Biochim Biophys Acta (Suppl.) , vol.12 , pp. 119
    • Sedlák, E.1    Robinson, N.C.2
  • 59
    • 31044445705 scopus 로고    scopus 로고
    • Photolabeling of cardiolipin binding subunits within bovine heart cytochromec oxidase
    • Sedlák E, Panda M, Dale MP, Weintraub ST, Robinson NC. Photolabeling of cardiolipin binding subunits within bovine heart cytochromec oxidase. Biochemistry 2006; 45: 746-754.
    • (2006) Biochemistry , vol.45 , pp. 746-754
    • Sedlák, E.1    Panda, M.2    Dale, M.P.3    Weintraub, S.T.4    Robinson, N.C.5
  • 60
    • 4243621072 scopus 로고    scopus 로고
    • Lipid peroxidation
    • In: Yu BP (ed). Boca Raton, FL: CRC Press
    • Matsuo M, Kaneko T. Lipid peroxidation. In: Yu BP (ed). Methods in aging research. Boca Raton, FL: CRC Press; 1998. pp. 571-606.
    • (1998) Methods in Aging Research , pp. 571-606
    • Matsuo, M.1    Kaneko, T.2
  • 62
    • 33745270756 scopus 로고    scopus 로고
    • Contribution of peroxidized cardiolipin to inactivation of bovine heart cytochromec oxidase
    • Musatov A. Contribution of peroxidized cardiolipin to inactivation of bovine heart cytochromec oxidase. Free Radic Biol Med 2006; 41: 238-246.
    • (2006) Free Radic Biol Med , vol.41 , pp. 238-246
    • Musatov, A.1
  • 63
    • 0025146398 scopus 로고
    • Cardiolipin-depleted bovine heart cytochromec oxidase: Binding stoichiometry and affi nity for cardiolipin derivatives
    • Robinson NC, Zborowski J, Talbert LH. Cardiolipin-depleted bovine heart cytochromec oxidase: binding stoichiometry and affi nity for cardiolipin derivatives. Biochemistry 1990; 29: 8962-8969.
    • (1990) Biochemistry , vol.29 , pp. 8962-8969
    • Robinson, N.C.1    Zborowski, J.2    Talbert, L.H.3
  • 64
    • 0037172778 scopus 로고    scopus 로고
    • Identifi cation of bovine heart cytochromec oxidase subunits modifi ed by the lipid peroxidation product 4-hydroxy-2 nonenal
    • Musatov A, Carrol CA, Liu YC, Henderson GI, Weintraub ST, Robinson NC. Identifi cation of bovine heart cytochromec oxidase subunits modifi ed by the lipid peroxidation product 4-hydroxy-2 nonenal. Biochemistry 2002; 41: 8212-8229.
    • (2002) Biochemistry , vol.41 , pp. 8212-8229
    • Musatov, A.1    Carrol, C.A.2    Liu, Y.C.3    Henderson, G.I.4    Weintraub, S.T.5    Robinson, N.C.6
  • 65
    • 0032496339 scopus 로고
    • Inhibition of cytochromec oxidase activity by 4-hydroxynonenal (HNE): Role of HNE adduct formation with the enzyme subunits
    • Chen J, Schenker S, Frosto TA, Henderson GI. Inhibition of cytochromec oxidase activity by 4-hydroxynonenal (HNE): role of HNE adduct formation with the enzyme subunits. Biochim Biophys Acta 1988; 1380: 336-344.
    • (1988) Biochim Biophys Acta , vol.1380 , pp. 336-344
    • Chen, J.1    Schenker, S.2    Frosto, T.A.3    Henderson, G.I.4
  • 66
    • 0032996250 scopus 로고    scopus 로고
    • Formation of 4-hydroxynonenal adducts with cytochromec oxidase in rats following short-term ethanol intake
    • Chen J, Robinson NC, Schenker S, Frosto TA, Henderson GI. Formation of 4-hydroxynonenal adducts with cytochromec oxidase in rats following short-term ethanol intake. Hepatology 1999; 29: 1792-1798.
    • (1999) Hepatology , vol.29 , pp. 1792-1798
    • Chen, J.1    Robinson, N.C.2    Schenker, S.3    Frosto, T.A.4    Henderson, G.I.5
  • 67
    • 0035196175 scopus 로고    scopus 로고
    • Role of 4-hydroxynonenal in modifi cation of cytochromec oxidase in ischemia/reperfused rat heart
    • Chen J, Henderson GI, Freeman GL. Role of 4-hydroxynonenal in modifi cation of cytochromec oxidase in ischemia/reperfused rat heart. J Mol Cell Cardiol 2001; 33: 1919-1927.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1919-1927
    • Chen, J.1    Henderson, G.I.2    Freeman, G.L.3
  • 69
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • Humphries KM, Szweda LI. Selective inactivation of-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 1998; 37: 15835-15841.
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 70
    • 0034060591 scopus 로고    scopus 로고
    • Formation of malondialdehyde adducts in livers of rats exposed to ethanol: Role in ethanol-mediated inhibition of cytochromec oxidase
    • Chen J, Petersen DR, Schenker S, Henderson GI. Formation of malondialdehyde adducts in livers of rats exposed to ethanol: role in ethanol-mediated inhibition of cytochromec oxidase. Alcohol Clin Exp Res 2000; 24: 544-552.
    • (2000) Alcohol Clin Exp Res , vol.24 , pp. 544-552
    • Chen, J.1    Petersen, D.R.2    Schenker, S.3    Henderson, G.I.4
  • 71
    • 33747345594 scopus 로고    scopus 로고
    • Malonaldehyde acts as a mitochondrial toxin: Inhibitory eff ects on respiratory function and enzyme activities in isolated rat liver mitochondria
    • Long J, Wang X, Gao H, Liu Z, Liu C, Miao M, Liu J. Malonaldehyde acts as a mitochondrial toxin: inhibitory eff ects on respiratory function and enzyme activities in isolated rat liver mitochondria. Life Sci 2006; 79: 1466-1472.
    • (2006) Life Sci , vol.79 , pp. 1466-1472
    • Long, J.1    Wang, X.2    Gao, H.3    Liu, Z.4    Liu, C.5    Miao, M.6    Liu, J.7
  • 72
    • 0032775546 scopus 로고    scopus 로고
    • Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Serena D, Ruggiero FM. Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion. Free Radic Biol Med 1999; 27: 42-50.
    • (1999) Free Radic Biol Med , vol.27 , pp. 42-50
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Serena, D.5    Ruggiero, F.M.6
  • 74
    • 0034988397 scopus 로고    scopus 로고
    • Oxidative damage to mitochondria and aging
    • Van Remmen H, Richardson A. Oxidative damage to mitochondria and aging. Exp Gerontol 2001; 36: 957-968.
    • (2001) Exp Gerontol , vol.36 , pp. 957-968
    • Van Remmen, H.1    Richardson, A.2
  • 75
    • 32244448364 scopus 로고    scopus 로고
    • Alterations in mitochondrial function, hydrogen peroxide release and oxidative damage in mouse hind-limb skeletal muscle during aging
    • Mansouri A, Muller FL, Liu Y, Ng R, Faulkner J, Hamilton M, et al. Alterations in mitochondrial function, hydrogen peroxide release and oxidative damage in mouse hind-limb skeletal muscle during aging. Mech Ageing Dev 2006; 127: 298-306.
    • (2006) Mech Ageing Dev , vol.127 , pp. 298-306
    • Mansouri, A.1    Muller, F.L.2    Liu, Y.3    Ng, R.4    Faulkner, J.5    Hamilton, M.6
  • 76
    • 13944261237 scopus 로고    scopus 로고
    • Due to reverse electron transfer, mitochondrial H 2 O 2 release increases with age in human vastus lateralis muscle although oxidative capacity is preserve
    • Capela F, Rimbertb V, Liogerb D, Diota A, Roussetb P, Patureau Miranda P, et al. Due to reverse electron transfer, mitochondrial H 2 O 2 release increases with age in human vastus lateralis muscle although oxidative capacity is preserve. Mech Ageing Dev 2005; 126: 505-511.
    • (2005) Mech Ageing Dev , vol.126 , pp. 505-511
    • Capela, F.1    Rimbertb, V.2    Liogerb, D.3    Diota, A.4    Roussetb, P.5    Patureau Miranda, P.6
  • 77
    • 0030248727 scopus 로고    scopus 로고
    • Influences of age and dietary restriction on gastrocnemius electron transport system activities in mice
    • Desai VG, Weindruch R, Hart RW, Feuers RJ. Influences of age and dietary restriction on gastrocnemius electron transport system activities in mice. Arch Biochem Biophys 1996; 333: 145-151.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 145-151
    • Desai, V.G.1    Weindruch, R.2    Hart, R.W.3    Feuers, R.J.4
  • 78
    • 77957662932 scopus 로고    scopus 로고
    • Cytochrome c oxidase loses catalytic activity and structural integrity during the aging process in Drosophila melanogaster
    • Ren JC, Rebrin I, Klichko V, Orr WC, Sohal RS. Cytochrome c oxidase loses catalytic activity and structural integrity during the aging process in Drosophila melanogaster. Biochem Biophys Res Commun 2010; 401: 64-68.
    • (2010) Biochem Biophys Res Commun , vol.401 , pp. 64-68
    • Ren, J.C.1    Rebrin, I.2    Klichko, V.3    Orr, W.C.4    Sohal, R.S.5
  • 79
    • 46649104435 scopus 로고    scopus 로고
    • Age-related decrease in expression of mitochondrial DNA encoded subunits of cytochromec oxidase in Drosophila melanogaster
    • Sohal RS, Toroser D, Br é g è re C, Mockett RJ, Orr WC. Age-related decrease in expression of mitochondrial DNA encoded subunits of cytochromec oxidase in Drosophila melanogaster. Mech Ageing Dev 2008; 129: 558-561.
    • (2008) Mech Ageing Dev , vol.129 , pp. 558-561
    • Sohal, R.S.1    Toroser, D.2    Brégère, C.3    Mockett, R.J.4    Orr, W.C.5
  • 80
    • 33746039656 scopus 로고    scopus 로고
    • Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: On defects in the cytochromec oxidase complex and aldehyde detoxifi cation
    • Ohta S, Ohsawa I. Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: On defects in the cytochromec oxidase complex and aldehyde detoxifi cation. J Alzheimer's Dis 2006; 9: 155-166.
    • (2006) J Alzheimer's Dis , vol.9 , pp. 155-166
    • Ohta, S.1    Ohsawa, I.2
  • 81
    • 33644867986 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation modulates cytochromec oxidase function and augments hypoxia and myocardial ischemia-related injury
    • Prabu SK, Anandatheerthavarada HK, Raza H, Srinivasan S, Spear JF, Avadhani NG. Protein kinase A-mediated phosphorylation modulates cytochromec oxidase function and augments hypoxia and myocardial ischemia-related injury. J Biol Chem 2006; 281: 2061-2070.
    • (2006) J Biol Chem , vol.281 , pp. 2061-2070
    • Prabu, S.K.1    Anandatheerthavarada, H.K.2    Raza, H.3    Srinivasan, S.4    Spear, J.F.5    Avadhani, N.G.6
  • 82
    • 0020134086 scopus 로고
    • An investigation by EPR and optical spectroscopy of cytochrome oxidase during turnover
    • Wilson MT, Jensen P, Aasa R, Malmström PG, Vänngard T. An investigation by EPR and optical spectroscopy of cytochrome oxidase during turnover. Biochem J 1982; 203: 483-492.
    • (1982) Biochem J , vol.203 , pp. 483-492
    • Wilson, M.T.1    Jensen, P.2    Aasa, R.3    Malmström, P.G.4    Vänngard, T.5
  • 83
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 2003; 552: 335-344.
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 84
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria. Central role of complex III
    • Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, Lesnefsky EJ. Production of reactive oxygen species by mitochondria. Central role of complex III. J Biol Chem 2003; 278: 36027-36031.
    • (2003) J Biol Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 85
    • 63449139296 scopus 로고    scopus 로고
    • Degenerative diseases, oxidative stress and cytochromec oxidase function
    • Kadenbach B, Ramzan R, Vogt S. Degenerative diseases, oxidative stress and cytochromec oxidase function. Trends Mol Med 2009; 15: 139-147.
    • (2009) Trends Mol Med , vol.15 , pp. 139-147
    • Kadenbach, B.1    Ramzan, R.2    Vogt, S.3
  • 87
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochromec oxidase: Catalytic turnover in the absence of subunit III alters the active site
    • Bratton MR, Pressler MA, Hosler JP. Suicide inactivation of cytochromec oxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry 1999; 38: 16236-16245.
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 88
    • 0042847430 scopus 로고    scopus 로고
    • Reversible inhibition of cytochromec oxidase by peroxynitrite proceeds through ascorbate-dependent generation of nitric oxide
    • Barone MC, Darley-Usmar VM, Brookes PS. Reversible inhibition of cytochromec oxidase by peroxynitrite proceeds through ascorbate-dependent generation of nitric oxide. J Biol Chem 2003; 278: 27520-27524.
    • (2003) J Biol Chem , vol.278 , pp. 27520-27524
    • Barone, M.C.1    Darley-Usmar, V.M.2    Brookes, P.S.3
  • 89
    • 77957756053 scopus 로고    scopus 로고
    • Ferricytochromec protects mitochondrial cytochromec oxidase against hydrogen peroxide-induced oxidative damage
    • Sedlák E, Fabian M, Robinson NC, Musatov A. Ferricytochromec protects mitochondrial cytochromec oxidase against hydrogen peroxide-induced oxidative damage. Free Radic Biol Med 2010; 49: 1574-1581.
    • (2010) Free Radic Biol Med , vol.49 , pp. 1574-1581
    • Sedlák, E.1    Fabian, M.2    Robinson, N.C.3    Musatov, A.4
  • 90
  • 91
    • 0032479524 scopus 로고    scopus 로고
    • Complete structure of the 11-subunit bovine mitochondrial cytochrome bc 1 complex
    • Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, et al. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc 1 complex. Science 1998; 281: 64-71.
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1    Lee, J.W.2    Okada, K.3    Lee, J.K.4    Iwata, M.5    Rasmussen, B.6
  • 92
    • 0025358947 scopus 로고
    • The protonmotive Q cycle
    • Trumpower BL. The protonmotive Q cycle. J Biol Chem 1990; 265: 11409-1141.
    • (1990) J Biol Chem , vol.265 , pp. 11409-21141
    • Trumpower, B.L.1
  • 94
    • 0039843110 scopus 로고    scopus 로고
    • Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc 1
    • Gomez B Jr., Robinson NC. Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc 1. Biochemistry 1999; 38: 9031-9038.
    • (1999) Biochemistry , vol.38 , pp. 9031-9038
    • Gomez, Jr.B.1    Robinson, N.C.2
  • 95
    • 0035803487 scopus 로고    scopus 로고
    • Specifi c roles of protein-phospholipid interactions in the yeast cytochrome bc 1 complex structure
    • Lange C, Nett JH, Trumpower BL, Hunte C. Specifi c roles of protein-phospholipid interactions in the yeast cytochrome bc 1 complex structure. EMBO J 2001; 20: 6591-6600.
    • (2001) EMBO J , vol.20 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 96
    • 0142195820 scopus 로고    scopus 로고
    • Superoxide anion generation by the cytochrome bc 1 complex
    • Sun J, Trumpower BL. Superoxide anion generation by the cytochrome bc 1 complex. Arch Biochem Biophys 2003; 419: 198-206.
    • (2003) Arch Biochem Biophys , vol.419 , pp. 198-206
    • Sun, J.1    Trumpower, B.L.2
  • 97
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A, Oshino N, Chance B. The cellular production of hydrogen peroxide. Biochem J 1972; 128: 617-130.
    • (1972) Biochem J , vol.128 , pp. 617-130
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 98
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochromec reductase from bovine heart mitochondria
    • Zhang L, Yu L, Yu CA. Generation of superoxide anion by succinate-cytochromec reductase from bovine heart mitochondria. J Biol Chem 1998; 273: 33972-33976.
    • (1998) J Biol Chem , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3
  • 99
    • 77952768766 scopus 로고    scopus 로고
    • Reaction mechanism of superoxide generation durinGubiquinol oxidation by the cytochrome bc 1 complex
    • Yin Y, Yang S, Yu L, Yu CA. Reaction mechanism of superoxide generation durinGubiquinol oxidation by the cytochrome bc 1 complex. J Biol Chem 2010; 285: 17038-17045.
    • (2010) J Biol Chem , vol.285 , pp. 17038-17045
    • Yin, Y.1    Yang, S.2    Yu, L.3    Yu, C.A.4
  • 100
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller FL, Liu Y, Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane J Biol Chem 2004;279:49064-49073.
    • (2004) J Biol Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 101
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochromec release
    • Madesh M, Hajnó czky G. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochromec release. J Cell Biol 2001; 155: 1003-10015.
    • (2001) J Cell Biol , vol.155 , pp. 1003-10015
    • Madesh, M.1    Hajnóczky, G.2
  • 102
    • 0034770396 scopus 로고    scopus 로고
    • Ischemic injury to mitochondrial electron transport in the aging heart: Damage to the iron-sulfur protein subunit of electron transport complex III
    • Lesnefsky EJ, Gudz TI, Migita CT, Ikeda-Saito M, Hassan MO, Turkaly PJ, Hoppel CL. Ischemic injury to mitochondrial electron transport in the aging heart: damage to the iron-sulfur protein subunit of electron transport complex III. Arch Biochem Biophys 2001; 385: 117-128.
    • (2001) Arch Biochem Biophys , vol.385 , pp. 117-128
    • Lesnefsky, E.J.1    Gudz, T.I.2    Migita, C.T.3    Ikeda-Saito, M.4    Hassan, M.O.5    Turkaly, P.J.6    Hoppel, C.L.7
  • 103
    • 0037387920 scopus 로고    scopus 로고
    • Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: Role of reactive oxygen species and cardiolipin
    • Petrosillo G, Ruggiero FM, Di Venosa N, Paradies G. Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin. FASEB J 2003; 17: 714-716.
    • (2003) FASEB J , vol.17 , pp. 714-716
    • Petrosillo, G.1    Ruggiero, F.M.2    Di Venosa, N.3    Paradies, G.4
  • 105
    • 0035145954 scopus 로고    scopus 로고
    • Aging decreases electron transport complex III activity in heart interfi brillar mitochondria by alteration of the cytochromec binding site
    • Lesnefsky EJ, Gudz TI, Moghaddas S, Migita CT, Ikeda-Saito M, Turkaly PJ, Hoppel CL. Aging decreases electron transport complex III activity in heart interfi brillar mitochondria by alteration of the cytochromec binding site. J Mol Cell Cardiol 2001; 33: 37-41.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 37-41
    • Lesnefsky, E.J.1    Gudz, T.I.2    Moghaddas, S.3    Migita, C.T.4    Ikeda-Saito, M.5    Turkaly, P.J.6    Hoppel, C.L.7
  • 106
    • 0038367809 scopus 로고    scopus 로고
    • Aging defect at the Q O site of complex III augments oxyradical production in rat heart interfi brillar mitochondria
    • Moghaddas S, Hoppel CL, Lesnefsky EJ. Aging defect at the Q O site of complex III augments oxyradical production in rat heart interfi brillar mitochondria. Arch Biochem Biophys 2003; 414: 59-66.
    • (2003) Arch Biochem Biophys , vol.414 , pp. 59-66
    • Moghaddas, S.1    Hoppel, C.L.2    Lesnefsky, E.J.3
  • 107
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro L, Rodriguez M, Radi R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J Biol Chem 1994; 269: 29409-29415.
    • (1994) J Biol Chem , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 108
    • 27644434041 scopus 로고    scopus 로고
    • Nitrosative stress results in irreversible inhibition of purifi ed complexes i and III without modifi cation of cofactors
    • Pearce LL, Kanai AJ, Epperly MW, Peterson J. Nitrosative stress results in irreversible inhibition of purifi ed complexes I and III without modifi cation of cofactors. Nitric Oxide 2005; 13: 254-263.
    • (2005) Nitric Oxide , vol.13 , pp. 254-263
    • Pearce, L.L.1    Kanai, A.J.2    Epperly, M.W.3    Peterson, J.4
  • 109
    • 0033034787 scopus 로고    scopus 로고
    • 4-Hydroxy-2(E)-nonenal inhibits CNS mitochondrial respiration at multiple sites
    • Picklo MJ, Amarnath V, McIntyre JO, Graham DG, Montine TJ. 4-Hydroxy-2(E)-nonenal inhibits CNS mitochondrial respiration at multiple sites. J Neurochem 1999; 72: 1617-1624.
    • (1999) J Neurochem , vol.72 , pp. 1617-1624
    • Picklo, M.J.1    Amarnath, V.2    McIntyre, J.O.3    Graham, D.G.4    Montine, T.J.5
  • 110
    • 62349129124 scopus 로고    scopus 로고
    • Neuronal mitochondrial toxicity of malondialdehyde: Inhibitory eff ects on respiratory function and enzyme activities in rat brain mitochondria
    • Long J, Liu C, Sun L, Gao H, Liu J. Neuronal mitochondrial toxicity of malondialdehyde: inhibitory eff ects on respiratory function and enzyme activities in rat brain mitochondria. Neurochem Res 2009; 34: 786-794.
    • (2009) Neurochem Res , vol.34 , pp. 786-794
    • Long, J.1    Liu, C.2    Sun, L.3    Gao, H.4    Liu, J.5
  • 111
    • 67749111889 scopus 로고    scopus 로고
    • Membrane potential greatly enhances superoxide generation by the cytochrome bc 1 complex reconstituted into phospholipid vesicles
    • Rottenberg H, Covian R, Trumpower BL. Membrane potential greatly enhances superoxide generation by the cytochrome bc 1 complex reconstituted into phospholipid vesicles. J Biol Chem 2009; 284: 19203-19210.
    • (2009) J Biol Chem , vol.284 , pp. 19203-19210
    • Rottenberg, H.1    Covian, R.2    Trumpower, B.L.3
  • 112
    • 79955954490 scopus 로고    scopus 로고
    • Loss of a conserved tyrosine residue of cytochrome b induces reactive oxygen species production by cytochrome bc1
    • Lee DW, Selamoglu N, Lanciano P, Cooley JW, Forquer I, Kramer DM, Daldal F. Loss of a conserved tyrosine residue of cytochrome b induces reactive oxygen species production by cytochrome bc1. J Biol Chem 2011; 286; 18139-18148.
    • (2011) J Biol Chem , vol.286 , pp. 18139-18148
    • Lee, D.W.1    Selamoglu, N.2    Lanciano, P.3    Cooley, J.W.4    Forquer, I.5    Kramer, D.M.6    Daldal, F.7
  • 113
    • 0027104114 scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 1992; 25: 253-324.
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 114
    • 0025760073 scopus 로고
    • The respiratorychain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H, Friedrich T, Hofhaus G, Preis D. The respiratorychain NADH dehydrogenase (complex I) of mitochondria. Eur J Biochem 1991; 197: 563-576.
    • (1991) Eur J Biochem , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 116
    • 52049115385 scopus 로고    scopus 로고
    • Subunit analysis of bovine heart complex i by reversed-phase HPLC, ESI-MS/MS and MALDITOF mass spectrometry
    • Lemma-Gray P, Valušov á E, Carroll CA, Weintraub ST, Musatov A, Robinson NC. Subunit analysis of bovine heart complex I by reversed-phase HPLC, ESI-MS/MS and MALDITOF mass spectrometry. Anal Biochem 2008; 382: 116-121.
    • (2008) Anal Biochem , vol.382 , pp. 116-121
    • Lemma-Gray, P.1    Valušová, E.2    Carroll, C.A.3    Weintraub, S.T.4    Musatov, A.5    Robinson, N.C.6
  • 117
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • Hunte C, Zickermann V, Brandt U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 2010; 329: 448-451.
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 118
    • 80052097536 scopus 로고    scopus 로고
    • Respiratory complex I: 'Steam engine' of the cell
    • Efremov RG, Sazanov LA. Respiratory complex I: 'steam engine'of the cell? Curr Opin Struct Biol 2011; 21: 532-540.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 532-540
    • Efremov, R.G.1    Sazanov, L.A.2
  • 119
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complex i and III of the mitochondrial respiratory chain
    • Fry M, Green M. Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain. J Biol Chem 1981; 256: 1874-1880.
    • (1981) J Biol Chem , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, M.2
  • 120
    • 0037015686 scopus 로고    scopus 로고
    • Full recovery of the NADH:ubiquinone activity of complex i (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids
    • Dröse S, Zwicker K, Brandt U. Full recovery of the NADH:ubiquinone activity of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids. Biochim Biophys Acta 2002; 1556: 65-67.
    • (2002) Biochim Biophys Acta , vol.1556 , pp. 65-67
    • Dröse, S.1    Zwicker, K.2    Brandt, U.3
  • 121
    • 30144445462 scopus 로고    scopus 로고
    • Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria
    • Sharpley MS, Shannon RJ, Draghi F, Hirst J. Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria. Biochemistry 2006; 45: 241-248.
    • (2006) Biochemistry , vol.45 , pp. 241-248
    • Sharpley, M.S.1    Shannon, R.J.2    Draghi, F.3    Hirst, J.4
  • 122
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schägger H, Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J Biol Chem 2001; 276: 37861-37867.
    • (2001) J Biol Chem , vol.276 , pp. 37861-37867
    • Schägger, H.1    Pfeiffer, K.2
  • 123
    • 0028827252 scopus 로고
    • Dilated cardiomyophathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Li Y, Huang TT, Carlson EJ, Melov S, Ursell PC, Olson JL, et al. Dilated cardiomyophathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 1995; 11: 376-381.
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3    Melov, S.4    Ursell, P.C.5    Olson, J.L.6
  • 124
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S, Robinson BH. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 2000; 25: 502-508.
    • (2000) Trends Biochem Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 125
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell 2005; 120: 483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 126
    • 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 ML, Ventura B, Giuliano G, Bovina C, Formiggini G, Castelli GP, 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 2001; 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    Castelli, G.P.6    Lenaz, G.7
  • 127
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADHubiquinone reductase and ubiquinol-cytochromec reductase from beef-heart mitochondria
    • Cadenas E, Boveris A, Ragan CI, Stoppani AO. Production of superoxide radicals and hydrogen peroxide by NADHubiquinone reductase and ubiquinol-cytochromec reductase from beef-heart mitochondria. Arch Biochem Biophys 1977; 180: 248-257.
    • (1977) Arch Biochem Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 128
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul L, Hirst J. The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc Natl Acad Sci USA 2006; 103: 7607-7612.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 129
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species aff ect mitochondrial electron transport complex i activity through oxidative cardiolipin damage
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM. Reactive oxygen species aff ect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 2002; 286: 135-141.
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 130
    • 0346059551 scopus 로고    scopus 로고
    • Decrease in mitochondrial complex i activity in ischemic/reperfused rat heart involvement of reactive oxygen species and cardiolipin
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Federici A, Ruggiero FM. Decrease in mitochondrial complex I activity in ischemic/reperfused rat heart involvement of reactive oxygen species and cardiolipin. Circ Res 2004; 94: 53-59.
    • (2004) Circ Res , vol.94 , pp. 53-59
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Federici, A.5    Ruggiero, F.M.6
  • 131
    • 3142616357 scopus 로고    scopus 로고
    • Modulation of mitochondrial complex i activity by reversible Ca 2-and NADH mediated superoxide anion dependent inhibition
    • Sadek HA, Szweda PA, Szweda LI. Modulation of mitochondrial complex I activity by reversible Ca 2-and NADH mediated superoxide anion dependent inhibition. Biochemistry 2004; 43: 8494-8502.
    • (2004) Biochemistry , vol.43 , pp. 8494-8502
    • Sadek, H.A.1    Szweda, P.A.2    Szweda, L.I.3
  • 132
    • 0037716926 scopus 로고    scopus 로고
    • Ca2-induced oxidative stress in brain mitochondria treated with the respiratory chain inhibitor rotenone
    • Sousa SC, Maciel EN, Vercesi AE, Castilho RF. Ca2-induced oxidative stress in brain mitochondria treated with the respiratory chain inhibitor rotenone. FEBS Lett 2003; 543: 179-183.
    • (2003) FEBS Lett , vol.543 , pp. 179-183
    • Sousa, S.C.1    MacIel, E.N.2    Vercesi, A.E.3    Castilho, R.F.4
  • 133
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex i by nitric oxide, peroxynitrite and Snitrosothiols
    • Brown GC, Borutaite V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and Snitrosothiols. Biochim Biophys Acta 2004; 1658: 44-49.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 134
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabó C, Ischiropoulos H, Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov 2007; 6: 662-680.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 662-680
    • Szabó, C.1    Ischiropoulos, H.2    Radi, R.3
  • 135
    • 0034663637 scopus 로고    scopus 로고
    • Reversal of nitric oxide-, peroxynitrite-and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex i activity by light and thiols
    • Borutaite V, Budriunaite A, Brown GC. Reversal of nitric oxide-, peroxynitrite-and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light and thiols. Biochim Biophys Acta 2000; 1459: 405-412.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 405-412
    • Borutaite, V.1    Budriunaite, A.2    Brown, G.C.3
  • 136
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation
    • Riobo NA, Clementi E, Melani M, Boveris A, Cadenas E, Moncada S, Poderoso JJ. Nitric oxide inhibits mitochondrial NADH: ubiquinone reductase activity through peroxynitrite formation. Biochem J 2001; 359: 139-145.
    • (2001) Biochem J , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 137
    • 77749316875 scopus 로고    scopus 로고
    • Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage
    • Requejo R, Hurd TR, Costa NJ, Murphy MP. Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage. FEBS J 2010; 277: 1465-1480.
    • (2010) FEBS J , vol.277 , pp. 1465-1480
    • Requejo, R.1    Hurd, T.R.2    Costa, N.J.3    Murphy, M.P.4
  • 139
    • 79959731297 scopus 로고    scopus 로고
    • Why does mitochondrial complex i have so many subunits
    • Hirst J. Why does mitochondrial complex I have so many subunits? Biochem J 2011; 437: e1-e3.
    • (2011) Biochem J , vol.437
    • Hirst, J.1
  • 140
    • 0036489190 scopus 로고    scopus 로고
    • Control of oxygen free radical formation from mitochondrial complex I: Roles for protein kinase A and pyruvate dehydrogenase kinase
    • Raha S, Myint AT, Johnstone L, Robinson BH. Control of oxygen free radical formation from mitochondrial complex I: roles for protein kinase A and pyruvate dehydrogenase kinase. Free Radic Biol Med 2002; 32: 421-430.
    • (2002) Free Radic Biol Med , vol.32 , pp. 421-430
    • Raha, S.1    Myint, A.T.2    Johnstone, L.3    Robinson, B.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.