Yin and Yang of mitochondrial ROS

Oxidative Stress, Disease and Cancer

Volumn , Issue , 2006, Pages 1-60

  Starkov, Anatoly ^a   Wallace, Kendall B ^b  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84967683966     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/9781860948046_0001     Document Type: Chapter

References (211)

1. Turrens JF. Mitochondrial formation of reactive oxygen species. J. Physiol. 552: 335-344 (2003).
2. Nishino H, Ito A. Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver. J. Biochem. (Tokyo) 100: 1523-1531 (1986).
3. Lee JS, Huh WK, Lee BH, Baek YU, Hwang CS, Kim ST, Kim YR, Kang SO. Mitochondrial NADH-cytochrome b(5) reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1527: 31-38 (2001).
4. Whatley SA, Curti D, Marchbanks RM. Mitochondrial involvement in schizophrenia and other functional psychoses. Neurochem. Res. 21: 995-1004 (1996).
5. Whatley SA, Curti D, Das Gupta F, Ferrier IN, Jones S, Taylor C, Marchbanks RM. Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normal and schizophrenic patients. Mol. Psychiatry 3: 227-237 (1998).
6. Hauptmann N, Grimsby J, Shih JC, Cadenas E. The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Arch. Biochem. Biophys. 335: 295-304 (1996).
7. Simonson SG, Zhang J, Canada AT, Jr, Su YF, Benveniste H, Piantadosi CA. Hydrogen peroxide production bymonoamine oxidase during ischemiareperfusion in the rat brain. J. Cereb. Blood Flow Metab. 13: 125-134 (1993).
8. Kunduzova OR, Bianchi P, Parini A, Cambon C. Hydrogen peroxide production bymonoamine oxidase during ischemia/reperfusion. Eur. J. Pharmacol. 448: 225-230 (2002).
9. Maurel A, Hernandez C, Kunduzova O, Bompart G, Cambon C, Parini A, Frances B. Age-dependent increase in hydrogen peroxide production by cardiac monoamine oxidase A in rats. Am. J. Physiol. Heart Circ. Physiol. 284: H1460-1467 (2003).
10. Carvalho F, Duarte JA, Neuparth MJ, Carmo H, Fernandes E, Remiao F, Bastos ML. Hydrogen peroxide production in mouse tissues after acute d-amphetamine administration. Influence of monoamine oxidase inhibition. Arch. Toxicol. 75: 465-469 (2001).
11. Kumar MJ, Nicholls DG, Andersen JK. Oxidative alpha-ketoglutarate ehydrogenase inhibition via subtle elevations in monoamine oxidase B levels results in loss of spare respiratory capacity: implications for Parkinson’s disease. J. Biol. Chem. 278: 46432-46439 (2003).
12. Loffler M, Becker C, Wegerle E, Schuster G. Catalytic enzyme histochemistry and biochemical analysis of dihydroorotate dehydrogenase/oxidase and succinate dehydrogenase in mammalian tissues, cells and mitochondria. Histochem. Cell. Biol. 105: 119-128 (1996).
13. Forman JH, Kennedy J. Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid. J. Biol. Chem. 250: 4322-4326 (1975).
14. Forman HJ, Kennedy J. Dihydroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase. Arch. Biochem. Biophys. 173: 219-224 (1976).
15. Dileepan KN, Kennedy J. Complete inhibition of dihydro-orotate oxidation and superoxide production by 1,1,1-trifluoro-3-thenoylacetone in rat liver mitochondria. Biochem. J. 225: 189-194 (1985).
16. Brown LJ, Koza RA, Everett C, Reitman ML, Marshall L, Fahien LA, Kozak LP, MacDonald MJ. Normal thyroid thermogenesis but reduced viability and adiposity in mice lacking the mitochondrial glycerol phosphate dehydrogenase. J. Biol. Chem. 277: 32892-32898 (2002).
17. Lee YP, Lardy HA. Influence of thyroid hormones on L-alpha-glycerophosphate dehydrogenases and other dehydrogenases in various organs of the rat. J. Biol. Chem. 240: 1427-1436 (1965).
18. Dummler K, Muller S, Seitz HJ. Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues. Biochem. J. 317 (Pt 3): 913-918 (1996).
19. Koza RA, Kozak UC, Brown LJ, Leiter EH, MacDonald MJ, Kozak LP. Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase. Arch. Biochem. Biophys. 336: 97-104 (1996).
20. Estabrook RW, Sacktor B. Alpha-Glycerophosphate oxidase of flight muscle mitochondria. J. Biol. Chem. 233: 1014-1019 (1958).
21. Kwong LK, Sohal RS. Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch. Biochem. Biophys. 350: 118-126 (1998).
22. Miwa S, St-Pierre J, Partridge L, Brand MD. Superoxide and hydrogen peroxide production by Drosophila mitochondria. Free Radic. Biol. Med. 35: 938-948 (2003).
23. Zhang L, Yu L, Yu CA. Generation of superoxide anion by succinatecytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273: 33972-33976 (1998a).
24. McLennan HR, Degli Esposti M. The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species. J. Bioenerg. Biomembr. 32: 153-162 (2000).
25. Gardner PR. Aconitase: sensitive target and measure of superoxide. Methods Enzymol. 349: 9-23 (2002).
26. Vasquez-Vivar J, Kalyanaraman B, Kennedy MC. Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J. Biol. Chem. 275: 14064-14069 (2000).
27. Maas E, Bisswanger H. Localization of the alpha-oxoacid dehydrogenase multienzyme complexes within the mitochondrion. FEBS Lett. 277: 189-190 (1990).
28. Starkov AA, Fiskum G, Chinopoulos C, Lorenzo BJ, Browne SE, Patel MS, Beal MF. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. J. Neurosci. 24: 7779-7788 (2004).
29. Tretter L. Adam-Vizi V. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutaratedehydrogenase. J. Neurosci. 24: 7771-7778 (2004).
30. Bunik VI, Sievers C. Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 269: 5004-5015 (2002).
31. Turrens JF. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep. 17: 3-8 (1997).
32. Lenaz G. The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life 52: 159-164 (2001).
33. Kushnareva Y, Murphy AN, Andreyev A. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368: 545-553 (2002).
34. Liu Y, Fiskum G, Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80: 780-787 (2002).
35. Cadenas E, Boveris A, Ragan CI, Stoppani AO. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinolcytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180: 248-257 (1977).
36. Genova ML, Pich MM, Biondi A, Bernacchia A, Falasca A, Bovina C, Formiggini G, Parenti Castelli G, Lenaz G. Mitochondrial production of oxygen radical species and the role of coenzyme Q as an antioxidant. Exp. Biol. Med. (Maywood) 228: 506-513 (2003).
37. Hinkle PC, Butow RA, Racker E, Chance B. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles. J. Biol. Chem. 242: 5169-5173 (1967).
38. Takeshige K, Minakami S. NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J. 180: 129-135 (1979).
39. Herrero A, Barja G. Localization of the site of oxygen radical generation inside the complex I of heart and non-synaptic brain mammalian mitochondria. J. Bioenerg. Biomembr. 32: 609-615 (2000).
40. Genova ML, Ventura B, Giuliano G, Bovina C, Formiggini G, Parenti Castelli G, Lenaz G. The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably ironsulfur cluster N2. FEBS Lett. 505: 364-368 (2001).
41. Kang D, Narabayashi H, Sata T, Takeshige K. Kinetics of superoxide formation by respiratory chain NADH-dehydrogenase of bovine heart mitochondria. J. Biochem. (Tokyo) 94: 1301-1306 (1983).
42. Kudin AP, Bimpong-Buta NY, Vielhaber S, Elger CE, Kunz WS. Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem. 279: 4127-4135 (2004).
43. Krishnamoorthy G, Hinkle PC. Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase. J. Biol. Chem. 263: 17566-17575 (1988).
44. Korshunov SS, Skulachev VP, Starkov AA. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416: 15-18 (1997).
45. Hansford RG, Hogue BA, Mildaziene V. Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age. J. Bioenerg. Biomembr. 29: 89-95 (1997).
46. Votyakova TV, Reynolds IJ. DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 79: 266-277 (2001).
47. Starkov AA, Fiskum G. Regulation of brainmitochondrial H2O2 production by membrane potential and NAD(P)H redox state. J. Neurochem. 86: 1101-1107 (2003).
48. Lambert AJ, Brand MD. Superoxide production by NADH: ubiquinone oxidoreductase (complex I) depends on the pHgradient across the mitochondrial inner membrane. Biochem. J. 382: 511-517 (2004).
49. Turrens JF, Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191: 421-427 (1980).
50. Barja G. Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 31: 347-366 (1999).
51. Sipos I, Tretter L, Adam-Vizi V. Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals. J. Neurochem. 84: 112-118 (2003).
52. +. Biochem. Biophys. Res. Commun. 189: 47-52 (1992).
53. +: implications for neurodegeneration. J. Neurochem. 63: 584-591 (1994).
54. 2+-induced mitochondrial membrane permeabilization: role of coenzyme Q redox state. Am. J. Physiol. 269: C141-C147 (1995).
55. 2+ is dependent on mitochondrial-generated reactive oxygen species. FEBS Lett. 378: 150-152 (1996).
56. 2+. Arch. Biochem. Biophys. 359: 77-81 (1998b).
57. Kowaltowski AJ, Netto LE, Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J. Biol. Chem. 273: 12766-12769 (1998a).
58. 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. 278: 36027-36031 (2003).
59. Jensen PK. Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation. Biochim. Biophys. Acta 122: 157-166 (1966).
60. Loschen G, Azzi A, Richter C, Flohe L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett. 42: 68-72 (1974).
61. Dionisi O, Galeotti T, Terranova T, Azzi A. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochim. Biophys. Acta 403: 292-300 (1975).
62. Boveris A, Cadenas E, Stoppani AO. Role of ubiquinonein the mitochondrial generation of hydrogen peroxide. Biochem. J. 156: 435-444 (1976).
63. Grigolava IV, Ksenzenko M, Konstantinob AA, Tikhonov AN, Kerimov TM. Tiron as a spin-trap for superoxide radicals produced by the respiratory chain of submitochondrial particles. Biokhimiia 45: 75-82 (1980).
64. Sawyer DT, Valentine JS. How super is superoxide? Acc. Chem. Res. 14: 393-400 (1981).
65. Trumpower BL. The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex. J. Biol. Chem. 265: 11409-11412 (1990).
66. Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH. Electron transfer by domain movement in cytochrome bc1. Nature 392: 677-684 (1998b).
67. Crofts AR, Barquera B, Gennis RB, Kuras R, Guergova-Kuras M, Berry EA. Mechanism of ubiquinol oxidation by the bc(1) complex: different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors. Biochemistry 38: 15807-15826 (1999).
68. Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, Jap BK. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. Science 281: 64-71 (1998).
69. Kim H, Xia D, Yu CA, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J. Inhibitor binding changes domain mobility in the iron-sulfur protein of the mitochondrial bc1 complex from bovine heart. Proc. Natl. Acad. Sci. USA 95: 8026-8033 (1998).
70. Boveris A, Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134: 707-716 (1973).
71. Ksenzenko M, Konstantinov AA, Khomutov GB, Tikhonov AN, Ruuge EK. Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain. FEBS Lett. 155: 19-24 (1983).
72. Turrens JF, Alexandre A, Lehninger AL. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237: 408-414 (1985).
73. Junemann S, Heathcote P, Rich PR. On the mechanism of quinol oxidation in the bc1 complex. J. Biol. Chem. 273: 21603-21607 (1998).
74. Konstantinov AA, Peskin AV, Popova E, Khomutov GB, Ruuge EK. Superoxide generation by the respiratory chain of tumor mitochondria. Biochim. Biophys. Acta 894: 1-10 (1987).
75. Zoccarato F, Cavallini L, Deana R, Alexandre A. Pathways of hydrogen peroxide generation in guinea pig cerebral cortex mitochondria. Biochem. Biophys. Res. Commun. 154: 727-734 (1988).
76. Raha S, McEachern GE, Myint AT, Robinson BH. Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase. Free Radic. Biol. Med. 29: 170-180 (2000).
77. 2 production from mitochondrial respiratory chain. Biochem. Biophys. Res. Commun. 281: 645-650 (2001).
78. 2 generation by submitochondrial particles in the presence of succinate and antimycin. FEBS Lett. 175: 105-108 (1984).
79. Muller F, Crofts AR, Kramer DM. Multiple Q-cycle bypass reactions at the Qo site of the cytochrome bc1 complex. Biochemistry 41: 7866-7874(2002).
80. Muller FL, Roberts AG, Bowman MK, Kramer DM. Architecture of the Qo site of the cytochrome bc1 complex probed by superoxide production. Biochemistry 42: 6493-6499 (2003).
81. Sun J, Trumpower BL. Superoxide anion generation by the cytochrome bc1 complex. Arch. Biochem. Biophys. 419: 198-206 (2003).
82. Nohl H, Hegner D. Do mitochondria produce oxygen radicals in vivo? Eur. J. Biochem. 82: 563-567 (1978).
83. Miller RW, Rapp U. The oxidation of catechols by reduced flavins and dehydrogenases. An electron spin resonance study of the kinetics and initial products of oxidation. J. Biol. Chem. 248: 6084-6090 (1973).
84. Lynch RE, Fridovich I. Permeation of the erythrocyte stroma by superoxide radical. J. Biol. Chem. 253: 4697-4699 (1978).
85. 2−•) radicals. Biochim. Biophys. Acta 778: 579-585 (1984).
86. Mao GD, Poznansky MJ. Electron spin resonance study on the permeability of superoxide radicals in lipid bilayers and biologicalmembranes. FEBS Lett. 305: 233-236 (1992).
87. Takahashi MA, Asada K. Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch. Biochem. Biophys. 226: 558-566 (1983).
88. Frimer AA, Strul G, Buch J, Gottlieb HE. Can superoxide organic chemistry be observed within the liposomal bilayer? Free Radic. Biol. Med. 20: 843-852 (1996).
89. Han D, Williams E, Cadenas E. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 353: 411-416 (2001).
90. St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277: 44784-44790 (2002).
91. 2 production in pigeon heart mitochondria. FEBS Lett. 18: 261-264 (1971).
92. Cadenas E, Boveris A. Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplementedmitochondria. Biochem. J. 188: 31-37 (1980).
93. Klingenberg M, Rottenberg H. Relation between the gradient of the ATP/ADP ratio and the membrane potential across the mitochondrial membrane. Eur. J. Biochem. 73: 125-130 (1977).
94. Nohl H, Gille L, Schonheit K, Liu Y. Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen. Free Radic. Biol. Med. 20: 207-213 (1996).
95. Skulachev VP. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29: 169-202 (1996).
96. Packer L, Weber SU, Rimbach G. Molecular aspects of alpha-tocotrienol antioxidant action and cell signalling. J. Nutr. 131: 369S-373S (2001).
97. Lass A, Forster MJ, Sohal RS. Effects of coenzyme Q10 and alpha-tocopherol administration on their tissue levels in the mouse: elevation of mitochondrial alpha-tocopherol by coenzyme Q10. Free Radic. Biol. Med. 26: 1375-1382 (1999).
98. Thomas JP, Maiorino M, Ursini F, Girotti AW. Protective action of phospholipid hydroperoxideglutathione peroxidase againstmembrane-damaging lipid peroxidation. In situ reduction of phospholipid and cholesterol hydroperoxides. J. Biol. Chem. 265: 454-461 (1990).
99. Maiorino M, Thomas JP, Girotti AW, Ursini F. Reactivity of phospholipid hydroperoxide glutathione peroxidase with membrane and lipoprotein lipid hydroperoxides. Free Radic. Res. Commun. 12-13 (Pt 1): 131-135 (1991).
100. Bao Y, Jemth P, Mannervik B, Williamson G. Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxidase and glutathione transferases. FEBS Lett. 410: 210-212 (1997).
101. Imai H, Nakagawa Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 34: 145-169 (2003).
102. Yant LJ, Ran Q, Rao L, Van Remmen H, Shibatani T, Belter JG, Motta L, Richardson A, Prolla TA. The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults. Free Radic. Biol. Med. 34: 496-502 (2003).
103. Arai M, Imai H, Koumura T, Yoshida M, Emoto K, Umeda M, Chiba N, Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays amajor role in preventing oxidative injury to cells. J. Biol. Chem. 274: 4924-4933 (1999).
104. Nomura K, Imai H, Koumura T, Kobayashi T, Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem. J. 351: 183-193 (2000).
105. Esposito LA, Kokoszka JE, Waymire KG, Cottrell B, MacGregor GR, Wallace DC. Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene. Free Radic. Biol. Med. 28: 754-766 (2000).
106. Knopp EA, Arndt TL, Eng KL, Caldwell M, LeBoeuf RC, Deeb SS, O’Brien KD. Murine phospholipid hydroperoxide glutathione peroxidase: cDNA sequence, tissue expression, and mapping. Mamm. Genome. 10: 601-605 (1999).
107. Pushpa-Rekha TR, Burdsall AL, Oleksa LM, Chisolm GM, Driscoll DM. Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J. Biol. Chem. 270: 26993-26999 (1995).
108. Panfili E, Sandri G, Ernster L. Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria. FEBS Lett. 290: 35-37 (1991).
109. Godeas C, Sandri G, Panfili E. Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria. Biochim. Biophys. Acta 1191: 147-150 (1994).
110. Gardner PR, Raineri I, Epstein LB, White CW. Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270: 13399-13405 (1995).
111. Li Y, Huang TT, Carlson EJ, Melov S, Ursell PC, Olson JL, Noble LJ, Yoshimura MP, Berger C, Chan PH et al. Dilated cardiomyopathyand neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 11: 376-381 (1995).
112. Lebovitz RM, Zhang H, Vogel H, Cartwright J, Jr, Dionne L, Lu N, Huang S, Matzuk MM. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. USA 93: 9782-9787 (1996).
113. Tsan MF, White JE, Caska B, Epstein CJ, Lee CY. Susceptibility of heterozygous MnSOD gene-knockout mice to oxygen toxicity. Am. J. Respir. Cell. Mol. Biol. 19: 114-120 (1998).
114. Jackson RM, Helton ES, Viera L, Ohman T. Survival, lung injury, and lung protein nitration in heterozygous MnSOD knockout mice in hyperoxia. Exp. Lung. Res. 25: 631-646 (1999).
115. Van Remmen H, Ikeno Y, Hamilton M, Pahlavani M, Wolf N, Thorpe SR, Alderson NL, Baynes JW, Epstein CJ, Huang TT, Nelson J, Strong R, Richardson A. Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging. Physiol. Genomics 16: 29-37 (2003).
116. Van Remmen H, Williams MD, Guo Z, Estlack L, Yang H, Carlson EJ, Epstein CJ, Huang TT, Richardson A. Knockout mice heterozygous for Sod2 show alterations in cardiac mitochondrial function and apoptosis. Am. J. Physiol. Heart. Circ. Physiol. 281: H1422-1432 (2001).
117. Williams MD, Van Remmen H, Conrad CC, Huang TT, Epstein CJ, Richardson A. Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J. Biol. Chem. 273: 28510-28515 (1998).
118. Van Remmen H, Salvador C, Yang H, Huang TT, Epstein CJ, Richardson A. Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse. Arch. Biochem. Biophys. 363: 91-97 (1999).
119. Raineri I, Carlson EJ, Gacayan R, Carra S, Oberley TD, Huang TT, Epstein CJ. Strain-dependent high-level expression of a transgene for manganese superoxide dismutase is associated with growth retardation and decreased fertility. Free Radic. Biol. Med. 31: 1018-1030 (2001).
120. Hackenbrock CR, Chazotte B, Gupte SS. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J. Bioenerg. Biomembr. 18: 331-368 (1986).
121. McCord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reactions. II. The mechanism of the mediation of cytochrome c reduction by a variety of electron carriers. J. Biol. Chem. 245: 1374-1377 (1970).
122. Korshunov SS, Krasnikov BF, Pereverzev MO, Skulachev VP. The antioxidant functions of cytochrome c. FEBS Lett. 462: 192-198 (1999).
123. Mailer K. Superoxide radical as electron donor for oxidative phosphorylation of ADP. Biochem. Biophys. Res. Commun. 170: 59-64 (1990).
124. Ho YS, Xiong Y, Ma W, Spector A, Ho DS. Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury. J. Biol. Chem. 279: 32804-32812 (2004).
125. Radi R, Turrens JF, Chang LY, Bush KM, Crapo JD, Freeman BA. Detection of catalase in rat heart mitochondria. J. Biol. Chem. 266: 22028-22034 (1991).
126. DelMaestro R, McDonald W. Subcellular localization of superoxide dismutases, glutathione peroxidase and catalase in developing rat cerebral cortex. Mech. Ageing. Dev. 48: 15-31 (1989).
127. 2 detoxification in in vivo conditions. Free Radic. Biol. Med. 33: 1260-1267 (2002).
128. Dringen R. Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62: 649-671 (2000).
129. Pastore A, Federici G, Bertini E, Piemonte F. Analysis of glutathione: implication in redox and detoxification. Clin. Chim. Acta 333: 19-39 (2003).
130. Wahllander A, Soboll S, Sies H, Linke I, Muller M. Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-Stransferases. FEBS Lett. 97: 138-140 (1979).
131. Griffith OW, Meister A. Origin and turnover of mitochondrial glutathione. Proc. Natl. Acad. Sci. USA 82: 4668-4672 (1985).
132. Martensson J, Lai JC, Meister A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function. Proc. Natl. Acad. Sci. USA 87: 7185-7189 (1990).
133. Chen Z, Lash LH. Evidence formitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers. J. Pharmacol. Exp. Ther. 285: 608-618 (1998).
134. Rebrin I, Kamzalov S, Sohal RS. Effects of age and caloric restriction on glutathione redox state in mice. Free Radic. Biol. Med. 35: 626-635 (2003).
135. Vogel R, Wiesinger H, Hamprecht B, Dringen R. The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required. Neurosci. Lett. 275: 97-100 (1999).
136. Boveris A, Cadenas E. Cellular Sources and Steady-State Levels of Reactive Oxygen Species. Marcel Dekker, New York, 1997.
137. Han D, Canali R, Rettori D, Kaplowitz N. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol. Pharmacol. 64: 1136-1144 (2003).
138. Raza H, Robin MA, Fang JK, Avadhani NG. Multiple isoforms of mitochondrial glutathione S-transferases and their differential induction under oxidative stress. Biochem. J. 366: 45-55 (2002).
139. Olafsdottir K, Reed DJ. Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment. Biochim. Biophys. Acta 964: 377-382 (1988).
140. Kozhemiakin LA, Bulavin DV, Udintsev AV, Smirnov VV. The subcellular distribution of the glutathione system enzymes in the brain tissue of the rat. Tsitologiia 35: 58-63 (1993).
141. Kelner MJ, Montoya MA. Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem. Biophys. Res. Commun. 269: 366-368 (2000).
142. 2+. J. Biol. Chem. 279: 4166-4174 (2004).
143. Hoek JB, Rydstrom J. Physiological roles of nicotinamide nucleotide transhydrogenase. Biochem. J. 254: 1-10 (1988).
144. Arkblad EL, Egorov M, Shakhparonov M, Romanova L, Polzikov M, Rydstrom J. Expression of proton-pumping nicotinamide nucleotide transhydrogenase in mouse, human brain and C elegans. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 133: 13-21 (2002).
145. Bernstine EG. Genetic control of mitochondrial malic enzyme in mouse brain. J. Biol. Chem. 254: 83-87 (1979).
146. Stein AM, Stein JH, Kirkman SK. Diphosphopyridine nucleotide specific isocitric dehydrogenase of mammalianmitochondria. I. On the roles of pyridine nucleotide transhydrogenase and the isocitric dehydrogenases in the respiration of mitochondria of normal and neoplastic tissues. Biochemistry 6: 1370-1379 (1967).
147. Kirsch M, De Groot H. NAD(P)H, a directly operating antioxidant? FASEB J. 15: 1569-1574 (2001).
148. Tischler ME, Hecht P, Williamson JR. Effect of ammonia on mitochondrial and cytosolic NADH and NADPH systems in isolated rat liver cells. FEBS Lett. 76: 99-104 (1977).
149. Lenzen S, Drinkgern J, Tiedge M. Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues. Free Radic. Biol. Med. 20: 463-466 (1996).
150. Utsunomiya H, Komatsu N, Yoshimura S, Tsutsumi Y, Watanabe K. Exact ultrastructural localization of glutathione peroxidase in normal rat hepatocytes: advantages of microwave fixation. J. Histochem. Cytochem. 39: 1167-1174 (1991).
151. Asayama K, Yokota S, Dobashi K, Hayashibe H, Kawaoi A, Nakazawa S. Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: quantitative analysis by postembedding method. Histochemistry 102: 213-219 (1994).
152. Esworthy RS, Ho YS, Chu FF. The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch. Biochem. Biophys. 340: 59-63 (1997).
153. Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59: 527-605 (1979).
154. Mirault ME, Tremblay A, Beaudoin N, Tremblay M. Overexpression of seleno-glutathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants. J. Biol. Chem. 266: 20752-20760 (1991).
155. Sies H, Sharov VS, Klotz LO, Briviba K. Glutathione peroxidase protects against peroxynitrite-mediated oxidations. Anewfunction for selenoproteins as peroxynitrite reductase. J. Biol. Chem. 272: 27812-27817 (1997).
156. 2 stress. Exp. Eye Res. 62: 521-540 (1996).
157. Cheng WH, Ho YS, Ross DA, Valentine BA, Combs GF, Lei XG. Cellular glutathione peroxidase knockout mice express normal levels of seleniumdependent plasma and phospholipid hydroperoxide glutathione peroxidases in various tissues. J. Nutr. 127: 1445-1450 (1997).
158. Ho YS, Magnenat JL, Bronson RT, Cao J, Gargano M, Sugawara M, Funk CD. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272: 16644-16651 (1997).
159. Cheng WH, Ho YS, Valentine BA, Ross DA, Combs GF, Jr, Lei XG. Cellular glutathione peroxidase is the mediator of body selenium to protect against paraquat lethality in transgenic mice. J. Nutr. 128: 1070-1076 (1998).
160. de Haan JB, Bladier C, Griffiths P, Kelner M, O’Shea RD, Cheung NS, Bronson RT, Silvestro MJ, Wild S, Zheng SS, Beart PM, Hertzog PJ, Kola I. Mice with a homozygous nullmutation for the most abundant glutathione peroxidase, Gpx1, showincreased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J. Biol. Chem. 273: 22528-22536 (1998).
161. Klivenyi P, Andreassen OA, Ferrante RJ, Dedeoglu A, Mueller G, Lancelot E, Bogdanov M, Andersen JK, Jiang D, Beal MF. Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitropropionic acid, and 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. J. Neurosci. 20: 1-7 (2000).
162. Zhang J, Graham DG, Montine TJ, Ho YS. Enhanced N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity in mice deficient in CuZn-superoxide dismutase or glutathione peroxidase. J. Neuropathol. Exp. Neurol. 59: 53-61 (2000).
163. Fujii J, Ikeda Y. Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein. Redox. Rep. 7: 123-130 (2002).
164. Wood ZA, Schroder E, Robin Harris J, Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28: 32-40 (2003).
165. Chae HZ, Kim HJ, Kang SW, Rhee SG. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45: 101-112 (1999).
166. Leyens G, Donnay I, Knoops B. Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 136: 943-955 (2003).
167. Araki M, Nanri H, Ejima K, Murasato Y, Fujiwara T, Nakashima Y, Ikeda M. Antioxidant function of the mitochondrial protein SP-22 in the cardiovascular system. J. Biol. Chem. 274: 2271-2278 (1999).
168. Hattori F, Murayama N, Noshita T, Oikawa S. Mitochondrial peroxiredoxin-3 protects hippocampal neurons from excitotoxic injury in vivo. J. Neurochem. 86: 860-868 (2003).
169. Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, Knoops B. Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides. Free Radic. Biol. Med. 36: 65-77 (2004).
170. Johansson C, Lillig CH, Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 279: 7537-7543 (2004).
171. Fernandes AP, Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox. Signal 6: 63-74 (2004).
172. Gromer S, Urig S, Becker K. The thioredoxin system - from science to clinic. Med. Res. Rev. 24: 40-89 (2004).
173. Jurado J, Prieto-Alamo MJ, Madrid-Risquez J, Pueyo C. Absolute gene expression patterns of thioredoxin and glutaredoxin redox systems in mouse. J. Biol. Chem. 278: 45546-45554 (2003).
174. Nonn L, Williams RR, Erickson RP, Powis G. The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol. Cell. Biol. 23: 916-922 (2003).
175. Patenaude A, Murthy MR, Mirault ME. Mitochondrial thioredoxin system: effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis. J. Biol. Chem. 279: 27302-27314 (2004).
176. Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82: 47-95 (2002).
177. Pitkanen S, Robinson BH. Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase. J. Clin. Invest. 98: 345-351 (1996).
178. Swerdlow RH, Parks JK, Miller SW, Tuttle JB, Trimmer PA, Sheehan JP, Bennett JP, Jr, Davis RE, Parker WD, Jr. Origin and functional consequences of the complex I defect in Parkinson’s disease. Ann. Neurol. 40: 663-671 (1996).
179. Luo X, Pitkanen S, Kassovska-Bratinova S, Robinson BH, Lehotay DC. Excessive formation of hydroxyl radicals and aldehydic lipid peroxidation products in cultured skin fibroblasts from patients with complex I deficiency. J. Clin. Invest. 99: 2877-2882 (1997).
180. Barrientos A, Moraes CT. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274: 16188-16197 (1999).
181. Genova ML, Pich MM, Bernacchia A, Bianchi C, Biondi A, Bovina C, Falasca AI, Formiggini G, Castelli GP, Lenaz G. The mitochondrial production of reactive oxygen species in relation to aging and pathology. Ann. NY Acad. Sci. 1011: 86-100 (2004).
182. Rana M, de Coo I, Diaz F, Smeets H, Moraes CT. An out-of-frame cytochrome b gene deletion from a patient with Parkinsonism is associated with impaired complex III assembly and an increase in free radical production. Ann. Neurol. 48: 774-781 (2000).
183. Mattiazzi M, Vijayvergiya C, Gajewski CD, DeVivo DC, Lenaz G, Wiedmann M, Manfredi G. The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum. Mol. Genet. 13: 869-879 (2004).
184. Becker LB. New concepts in reactive oxygen species and cardiovascular reperfusion physiology. Cardiovasc. Res. 61: 461-470 (2004).
185. Ledenev AN, Ruuge EK. Generation of superoxide radicals by ischemic heart mitochondria. Bull. Eksp. Biol. Med. 100: 303-305 (1985).
186. Turrens JF, Beconi M, Barilla J, Chavez UB, McCord JM. Mitochondrial generation of oxygen radicals during reoxygenation of ischemic tissues. Free Radic. Res. Commun. 12-13 (Pt 2): 681-689 (1991).
187. 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. 17: 714-716 (2003).
188. 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. 94: 53-59 (2004).
189. Du G, Mouithys-Mickalad A, Sluse FE. Generation of superoxide anion by mitochondria and impairment of their functions during anoxia and reoxygenation in vitro. Free Radic. Biol. Med. 25: 1066-1074 (1998).
190. Cino M, Del Maestro RF. Generation of hydrogen peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia. Arch. Biochem. Biophys. 269: 623-638 (1989).
191. Dux E, Mies G, Hossmann KA, Siklos L. Calcium in the mitochondria following brief ischemia of gerbil brain. Neurosci. Lett. 78: 295-300 (1987).
192. Zaidan E, Sims NR. The calcium content of mitochondria from brain subregions following short-term forebrain ischemia and recirculation in the rat. J. Neurochem. 63: 1812-1819 (1994).
193. Fiskum G. Mitochondrial participation in ischemic and traumatic neural cell death. J. Neurotrauma. 17: 843-855 (2000).
194. Nicholls DG, Budd SL. Mitochondria and neuronal survival. Physiol. Rev. 80: 315-360 (2000).
195. Starkov AA, Polster BM, Fiskum G. Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax. J. Neurochem. 83: 220-228 (2002).
196. Hansford RG, Zorov D. Role of mitochondrial calcium transport in the control of substrate oxidation. Mol. Cell. Biochem. 184: 359-369 (1998).
197. Vandecasteele G, Szabadkai G, Rizzuto R. Mitochondrial calcium homeostasis: mechanisms and molecules. IUBMB Life 52: 213-219 (2001).
198. Lai JC, Cooper AJ. Brain alpha-ketoglutarate dehydrogenase complex: kinetic properties, regional distribution, and effects of inhibitors. J. Neurochem. 47: 1376-1386 (1986).
199. Lai JC, DiLorenzo JC, Sheu KF. Pyruvate dehydrogenase complex is inhibited in calcium-loaded cerebrocortical mitochondria. Neurochem. Res. 13: 1043-1048 (1988).
200. 2+. J. Biol. Chem. 255: 2457-2464 (1980).
201. Roman I, Clark A, Swanson PD. The interaction of calcium transport and ADP phosphorylation in brain mitochondria. Membr. Biochem. 4: 1-9 (1981).
202. Zoratti M, Szabo I. The mitochondrial permeability transition. Biochim. Biophys. Acta 1241: 139-176 (1995).
203. Lemasters JJ, Nieminen AL, Qian T, Trost LC, Herman B. Themitochondrial permeability transition in toxic, hypoxic and reperfusion injury. Mol. Cell. Biochem. 174: 159-165 (1997).
204. Lemasters JJ, Nieminen AL, Qian T, Trost LC, Elmore SP, Nishimura Y, Crowe RA, Cascio WE, Bradham CA, Brenner DA, Herman B. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim. Biophys. Acta 1366: 177-196 (1998).
205. Bernardi P, Scorrano L, Colonna R, Petronilli V, Di Lisa F. Mitochondria and cell death. Mechanistic aspects and methodological issues. Eur. J. Biochem. 264: 687-701 (1999).
206. He L, Lemasters JJ. Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function? FEBS Lett. 512: 1-7 (2002).
207. + and is a causative event in the death of myocytes in postischemic reperfusion of the heart. J. Biol. Chem. 276: 2571-2575 (2001).
208. Anderson MF, Sims NR. The effects of focal ischemia and reperfusion on the glutathione content of mitochondria fromrat brain subregions. J. Neurochem. 81: 541-549 (2002).
209. 2+-induced membrane permeability transition in brain mitochondria. J. Neurochem. 79: 1237-1245 (2001).
210. Perez Velazquez JL, Frantseva MV, Carlen PL. In vitro ischemia promotes glutamate-mediated free radical generation and intracellular calcium accumulation in hippocampal pyramidal neurons. J. Neurosci. 17: 9085-9094 (1997).
211. Zorov DB, Filburn CR, Klotz LO, Zweier JL, Sollott SJ. Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes. J. Exp. Med. 192: 1001-1014 (2000).