메뉴 건너뛰기




Volumn 1827, Issue 11-12, 2013, Pages 1332-1339

Molecular mechanisms of superoxide production by complex III: A bacterial versus human mitochondrial comparative case study

Author keywords

Complex III; Cytochrome bc1; Electron transfer; Mitochondria; Oxidative damages; Reactive oxygen species

Indexed keywords

CYTOCHROME B; MEMBRANE ENZYME; QUINONE DERIVATIVE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; TYROSINE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84884673437     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.03.009     Document Type: Review
Times cited : (64)

References (86)
  • 1
    • 33745198418 scopus 로고    scopus 로고
    • Redox regulation of cardiac calcium channels and transporters
    • A.V. Zima, and L.A. Blatter Redox regulation of cardiac calcium channels and transporters Cardiovasc. Res. 71 2006 310 321
    • (2006) Cardiovasc. Res. , vol.71 , pp. 310-321
    • Zima, A.V.1    Blatter, L.A.2
  • 2
    • 21344464962 scopus 로고    scopus 로고
    • 2+ sparks in permeabilized mammalian skeletal muscle
    • DOI 10.1113/jphysiol.2005.086280
    • 2 + sparks in permeabilized mammalian skeletal muscle J. Physiol. 565 2005 855 872 (Pubitemid 40903298)
    • (2005) Journal of Physiology , vol.565 , Issue.3 , pp. 855-872
    • Isaeva, E.V.1    Shkryl, V.M.2    Shirokova, N.3
  • 3
  • 4
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Dröge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95 (Pubitemid 34654215)
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Droge, W.1
  • 5
    • 1542619245 scopus 로고    scopus 로고
    • Reactive Oxygen Species as Mediators of Signal Transduction in Ischemic Preconditioning
    • DOI 10.1089/152308604322899521
    • H. Otani Reactive oxygen species as mediators of signal transduction in ischemic preconditioning Antioxid. Redox Signal. 6 2004 449 469 (Pubitemid 38332603)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.2 , pp. 449-469
    • Otani, H.1
  • 6
    • 78649391422 scopus 로고    scopus 로고
    • Cellular metabolic stress: Considering how cells respond to nutrient excess
    • K.E. Wellen, and C.B. Thompson Cellular metabolic stress: considering how cells respond to nutrient excess Mol. Cell 40 2010 323 332
    • (2010) Mol. Cell , vol.40 , pp. 323-332
    • Wellen, K.E.1    Thompson, C.B.2
  • 8
    • 0028032254 scopus 로고
    • Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines
    • J.M. Dypbukt, M. Ankarcrona, M. Burkitt, A. Sjöholm, K. Ström, S. Orrenius, and P. Nicotera Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines J. Biol. Chem. 269 1994 30553 30560
    • (1994) J. Biol. Chem. , vol.269 , pp. 30553-30560
    • Dypbukt, J.M.1    Ankarcrona, M.2    Burkitt, M.3    Sjöholm, A.4    Ström, K.5    Orrenius, S.6    Nicotera, P.7
  • 9
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence?
    • (Suppl.)
    • J.K. Andersen Oxidative stress in neurodegeneration: cause or consequence? Nat. Med. 10 2004 S18 S25 (Suppl.)
    • (2004) Nat. Med. , vol.10
    • Andersen, J.K.1
  • 10
    • 0034083227 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiovascular diseases
    • N.S. Dhalla, R.M. Temsah, and T. Netticadan Role of oxidative stress in cardiovascular diseases J. Hypertens. 18 2000 655 673 (Pubitemid 30406736)
    • (2000) Journal of Hypertension , vol.18 , Issue.6 , pp. 655-673
    • Dhalla, N.S.1    Temsah, R.M.2    Netticadan, T.3
  • 12
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • K.B. Beckman, and B.N. Ames The free radical theory of aging matures Physiol. Rev. 78 1998 547 581 (Pubitemid 28182903)
    • (1998) Physiological Reviews , vol.78 , Issue.2 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 13
    • 0035234813 scopus 로고    scopus 로고
    • A mitochondrial paradigm for degenerative diseases and ageing
    • D.C. Wallace A mitochondrial paradigm for degenerative diseases and ageing Novartis Found. Symp. 235 2001 247 263
    • (2001) Novartis Found. Symp. , vol.235 , pp. 247-263
    • Wallace, D.C.1
  • 15
    • 33745684904 scopus 로고    scopus 로고
    • Mitochondrial ROS-induced ROS release: An update and review
    • D.B. Zorov, M. Juhaszova, and S.J. Sollott Mitochondrial ROS-induced ROS release: an update and review Biochim. Biophys. Acta 1757 2006 509 517
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 509-517
    • Zorov, D.B.1    Juhaszova, M.2    Sollott, S.J.3
  • 16
    • 0034668833 scopus 로고    scopus 로고
    • Mitochondria and calcium: From cell signalling to cell death
    • M.R. Duchen Mitochondria and calcium: from cell signalling to cell death J. Physiol. 529 2000 57 68
    • (2000) J. Physiol. , vol.529 , pp. 57-68
    • Duchen, M.R.1
  • 17
    • 0030982120 scopus 로고    scopus 로고
    • The role of reactive oxygen species in mitochondrial permeability transition
    • DOI 10.1023/A:1027335217774
    • A.E. Vercesi, A.J. Kowaltowski, M.T. Grijalba, A.R. Meinicke, and R.F. Castilho The role of reactive oxygen species in mitochondrial permeability transition Biosci. Rep. 17 1997 43 52 (Pubitemid 27267591)
    • (1997) Bioscience Reports , vol.17 , Issue.1 , pp. 43-52
    • Vercesi, A.E.1    Kowaltowski, A.J.2    Grijalba, M.T.3    Meinicke, A.R.4    Castilho, R.F.5
  • 18
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • A. Osyczka, C.C. Moser, F. Daldal, and P.L. Dutton Reversible redox energy coupling in electron transfer chains Nature 427 2004 607 612 (Pubitemid 38248474)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 19
    • 80054965321 scopus 로고    scopus 로고
    • Reaction of superoxide radical with quinone molecules
    • R.I. Samoilova, A.R. Crofts, and S.A. Dikanov Reaction of superoxide radical with quinone molecules J. Phys. Chem. 115 2011 11589 11593
    • (2011) J. Phys. Chem. , vol.115 , pp. 11589-11593
    • Samoilova, R.I.1    Crofts, A.R.2    Dikanov, S.A.3
  • 21
    • 0035142151 scopus 로고    scopus 로고
    • Review: Mitochondrial medicine - Molecular pathology of defective oxidative phosphorylation
    • E. Fosslien Mitochondrial medicine-molecular pathology of defective oxidative phosphorylation Ann. Clin. Lab. Sci. 31 2001 25 67 (Pubitemid 32097212)
    • (2001) Annals of Clinical and Laboratory Science , vol.31 , Issue.1 , pp. 25-67
    • Fosslien, E.1
  • 22
    • 70449529407 scopus 로고    scopus 로고
    • Role of coenzyme Q10 (CoQ10) in cardiac disease, hypertension and Meniere-like syndrome
    • A. Kumar, H. Kaur, P. Devi, and V. Mohan Role of coenzyme Q10 (CoQ10) in cardiac disease, hypertension and Meniere-like syndrome Pharmacol. Ther. 124 2009 259 268
    • (2009) Pharmacol. Ther. , vol.124 , pp. 259-268
    • Kumar, A.1    Kaur, H.2    Devi, P.3    Mohan, V.4
  • 23
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: New approaches to an old problem of bioenergetics
    • V.P.V. Skulachev Uncoupling: new approaches to an old problem of bioenergetics Biochim. Biophys. Acta Bioenerg. 1363 1998 100 124
    • (1998) Biochim. Biophys. Acta Bioenerg. , vol.1363 , pp. 100-124
    • Skulachev, V.P.V.1
  • 24
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • A.A. Boveris, and B.B. Chance The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen Biochem. J. 134 1973 707 716
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.A.1    Chance, B.B.2
  • 25
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • A. Boveris, E. Cadenas, and A.O. Stoppani Role of ubiquinone in the mitochondrial generation of hydrogen peroxide Biochem. J. 156 1976 435 444
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 26
    • 34547098640 scopus 로고    scopus 로고
    • Fatty acids decrease mitochondrial generation of reactive oxygen species at the reverse electron transport but increase it at the forward transport
    • DOI 10.1016/j.bbabio.2007.04.005, PII S000527280700103X
    • P. Schönfeld, and L. Wojtczak Fatty acids decrease mitochondrial generation of reactive oxygen species at the reverse electron transport but increase it at the forward transport Biochim. Biophys. Acta 1767 2007 1032 1040 (Pubitemid 47101786)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.8 , pp. 1032-1040
    • Schonfeld, P.1    Wojtczak, L.2
  • 27
    • 84864540083 scopus 로고    scopus 로고
    • Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions
    • C.L. Quinlan, A.L. Orr, I.V. Perevoshchikova, J.R. Treberg, B.A. Ackrell, and M.D. Brand Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions J. Biol. Chem. 287 2012 27255 27264
    • (2012) J. Biol. Chem. , vol.287 , pp. 27255-27264
    • Quinlan, C.L.1    Orr, A.L.2    Perevoshchikova, I.V.3    Treberg, J.R.4    Ackrell, B.A.5    Brand, M.D.6
  • 28
    • 84867422702 scopus 로고    scopus 로고
    • Structural basis for malfunction in complex II
    • T.M. Iverson, E. Maklashina, and G. Cecchini Structural basis for malfunction in complex II J. Biol. Chem. 287 2012 35430 35438
    • (2012) J. Biol. Chem. , vol.287 , pp. 35430-35438
    • Iverson, T.M.1    Maklashina, E.2    Cecchini, G.3
  • 29
    • 0001875392 scopus 로고
    • Energy-linked reduction of mitochondrial pyridine nucleotide
    • B.B. Chance, and G.G. Hollunger Energy-linked reduction of mitochondrial pyridine nucleotide Nature 185 1960 666 672
    • (1960) Nature , vol.185 , pp. 666-672
    • Chance, B.B.1    Hollunger, G.G.2
  • 33
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • P. Mitchell Possible molecular mechanisms of the protonmotive function of cytochrome systems J. Theor. Biol. 62 1976 327 367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 34
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron transfer chain of Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism
    • A.R. Crofts, S.W. Meinhardt, K.R. Jones, and M. Snozzi The role of the quinone pool in the cyclic electron transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism Biochim. Biophys. Acta 723 1983 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
  • 42
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • DOI 10.1016/S0969-2126(00)00152-0
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment Structure 8 2000 669 684 (Pubitemid 30409318)
    • (2000) Structure , vol.8 , Issue.6 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 43
    • 46649119960 scopus 로고    scopus 로고
    • y fusion complexes reveal the distance constraints for functional electron transfer between photosynthesis components
    • y fusion complexes reveal the distance constraints for functional electron transfer between photosynthesis components J. Biol. Chem. 283 2008 13973 13982
    • (2008) J. Biol. Chem. , vol.283 , pp. 13973-13982
    • Lee, D.W.1    Ozturk, Y.2    Osyczka, A.3    Cooley, J.W.4    Daldal, F.5
  • 47
    • 0018971809 scopus 로고
    • Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate·cytochrome c reductase complex
    • T. Ohnishi, and B. Trumpower Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate: cytochrome c reductase complex J. Biol. Chem. 255 1980 3278 3284 (Pubitemid 10014659)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.8 , pp. 3278-3284
    • Ohnishi, T.1    Trumpower, B.L.2
  • 48
    • 0019326470 scopus 로고
    • 2: Cytochrome c oxidoreductase segment of the mitochondrial respiratory chain
    • 2:cytochrome c oxidoreductase segment of the mitochondrial respiratory chain FEBS Lett. 122 1980 143 148
    • (1980) FEBS Lett. , vol.122 , pp. 143-148
    • De Vries, S.1    Berden, J.A.2    Slater, E.C.3
  • 59
    • 80052419584 scopus 로고    scopus 로고
    • The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle
    • C.L. Quinlan, A.A. Gerencser, J.R. Treberg, and M.D. Brand The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle J. Biol. Chem. 286 2011 31361 31372
    • (2011) J. Biol. Chem. , vol.286 , pp. 31361-31372
    • Quinlan, C.L.1    Gerencser, A.A.2    Treberg, J.R.3    Brand, M.D.4
  • 60
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 1979 527 605 (Pubitemid 9236599)
    • (1979) Physiological Reviews , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 61
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
    • A. Boveris, and E. Cadenas Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration FEBS Lett. 54 1975 311 314
    • (1975) FEBS Lett. , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 62
    • 0019168007 scopus 로고
    • Identification of the BAL-labile factor
    • DOI 10.1038/288717a0
    • E.C. Slater, and S. de Vries Identification of the BAL-labile factor Nature 288 1980 717 718 (Pubitemid 11168530)
    • (1980) Nature , vol.288 , Issue.5792 , pp. 717-718
    • Slater, E.C.1    De Vries, S.2
  • 64
    • 39549102405 scopus 로고    scopus 로고
    • Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria
    • Q. Chen, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria AJP - Cell Physiol. 294 2008 C460 C466
    • (2008) AJP - Cell Physiol. , vol.294
    • Chen, Q.1    Moghaddas, S.2    Hoppel, C.L.3    Lesnefsky, E.J.4
  • 68
    • 47749126543 scopus 로고    scopus 로고
    • Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer
    • S. Solmaz, and C. Hunte Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer J. Biol. Chem. 283 2008 17542 17549
    • (2008) J. Biol. Chem. , vol.283 , pp. 17542-17549
    • Solmaz, S.1    Hunte, C.2
  • 72
    • 33746628483 scopus 로고    scopus 로고
    • Probing the role of E272 in quinol oxidation of mitochondrial complex III
    • DOI 10.1021/bi060280g
    • T. Wenz, P. Hellwig, F. MacMillan, B. Meunier, and C. Hunte Probing the role of E272 in quinol oxidation of mitochondrial complex III Biochemistry 45 2006 9042 9052 (Pubitemid 44156366)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9042-9052
    • Wenz, T.1    Hellwig, P.2    MacMillan, F.3    Meunier, B.4    Hunte, C.5
  • 76
    • 0034797268 scopus 로고    scopus 로고
    • Multisystem disorder associated with a missense mutation in the mitochondrial cytochrome b gene
    • DOI 10.1002/ana.1224
    • F. Wibrand, K. Ravn, M. Schwartz, T. Rosenberg, N. Horn, and J. Vissing Multisystem disorder associated with a missense mutation in the mitochondrial cytochrome b gene Ann. Neurol. 50 2001 540 543 (Pubitemid 32938901)
    • (2001) Annals of Neurology , vol.50 , Issue.4 , pp. 540-543
    • Wibrand, F.1    Ravn, K.2    Schwartz, M.3    Rosenberg, T.4    Horn, N.5    Vissing, J.6
  • 77
    • 81255210901 scopus 로고    scopus 로고
    • Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
    • T. Althoff, D.J. Mills, J.L. Popot, and W. Kuhlbrandt Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1 EMBO J. 30 2011 4652 4664
    • (2011) EMBO J. , vol.30 , pp. 4652-4664
    • Althoff, T.1    Mills, D.J.2    Popot, J.L.3    Kuhlbrandt, W.4
  • 78
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • S. Dröse, and U. Brandt Molecular mechanisms of superoxide production by the mitochondrial respiratory chain Adv. Exp. Med. Biol. 748 2012 145 169
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 145-169
    • Dröse, S.1    Brandt, U.2
  • 80
    • 77949634569 scopus 로고    scopus 로고
    • Structure and organization of mitochondrial respiratory complexes: A new understanding of an old subject
    • G. Lenaz, and M.L. Genova Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject Antioxid. Redox Signal. 12 2010 961 1008
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 961-1008
    • Lenaz, G.1    Genova, M.L.2
  • 85
    • 33748488683 scopus 로고    scopus 로고
    • Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus
    • DOI 10.1111/j.1365-2958.2006.05253.x
    • S. Aygun-Sunar, S. Mandaci, H.G. Koch, I.V. Murray, H. Goldfine, and F. Daldal Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus Mol. Microbiol. 61 2006 418 435 (Pubitemid 44356573)
    • (2006) Molecular Microbiology , vol.61 , Issue.2 , pp. 418-435
    • Aygun-Sunar, S.1    Mandaci, S.2    Koch, H.-G.3    Murray, I.V.J.4    Goldfine, H.5    Daldal, F.6
  • 86
    • 84872081577 scopus 로고    scopus 로고
    • Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV
    • S. Bazan, E. Mileykovskaya, V.K. Mallampalli, P. Heacock, G.C. Sparagna, and W. Dowhan Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV J. Biol. Chem. 288 2013 401 411
    • (2013) J. Biol. Chem. , vol.288 , pp. 401-411
    • Bazan, S.1    Mileykovskaya, E.2    Mallampalli, V.K.3    Heacock, P.4    Sparagna, G.C.5    Dowhan, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.