References
- Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002; 82: 47–95
- Ghezzi P, Bonetto V, Fratelli M. Thiol–disulfide balance: From the concept of oxidative stress to that of redox regulation. Antioxid Redox Signal 2005; 7: 964–972
- Rhee SG. Redox signaling: Hydrogen peroxide as intracellular messenger. Exp Mol Med 1999; 31: 53–59
- Shelton MD, Chock PB, Mieyal JJ. Glutaredoxin: Role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 2005; 7: 348–366
- Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 2000; 29: 222–230
- Nulton-Persson AC, Szweda LI. Modulation of mitochondrial function by hydrogen peroxide. J Biol Chem 2001; 276: 23357–23361
- Bulteau AL, Ikeda-Saito M, Szweda LI. Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry 2003; 42: 14846–14855
- Nulton-Persson AC, Starke DW, Mieyal JJ, Szweda LI. Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 2003; 42: 4235–4242
- Beinert H, Kennedy MC, Stout CD. Aconitase as iron-Sulfur protein, enzyme, and iron-regulatory protein. Chem Rev 1996; 96: 2335–2374
- Gardner PR. Aconitase: Sensitive target and measure of superoxide. Methods Enzymol 2002; 349: 9–23
- Vasquez-Vivar J, Kalyanaraman B, Kennedy MC. Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J Biol Chem 2000; 275: 14064–14069
- Verniquet F, Gaillard J, Neuburger M, Douce R. Rapid inactivation of plant aconitase by hydrogen peroxide. Biochem J 1991; 276: 643–648
- Bulteau AL, O'Neill HA, Kennedy MC, Ikeda-Saito M, Isaya G, Szweda LI. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 2004; 305: 242–245
- Bulteau AL, Lundberg KC, Ikeda-Saito M, Isaya G, Szweda LI. Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion. Proc Natl Acad Sci USA 2005; 102: 5987–5991
- Han D, Canali R, Garcia J, Aguilera R, Gallaher TK, Cadenas E. Sites and mechanisms of aconitase inactivation by peroxynitrite: Modulation by citrate and glutathione. Biochemistry 2005; 44: 11986–11996
- Bunik V, Follmann H, Bisswanger H. Activation of mitochondrial 2-oxoacid dehydrogenases by thioredoxin. Biol Chem 1997; 378: 1125–1130
- Bunik VI, Sievers C. Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur J Biochem 2002; 269: 5004–5015
- Bunik VI. 2-Oxo acid dehydrogenase complexes in redox regulation. Eur J Biochem 2003; 270: 1036–1042
- 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 2004; 24: 7779–7788
- Humphries KM, Yoo Y, Szweda LI. Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal. Biochemistry 1998; 37: 552–557
- Humphries KM, Szweda LI. Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 1998; 37: 15835–15841
- Beal MF. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann Neurol 1995; 38: 357–366
- Kish SJ. Brain energy metabolizing enzymes in Alzheimer's disease: Alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase. Ann N Y Acad Sci 1997; 826: 218–228
- Mastrogiacomo F, Bergeron C, Kish SJ. Brain alpha-ketoglutarate dehydrogenase complex activity in Alzheimer's disease. J Neurochem 1993; 61: 2007–2014
- Lucas DT, Szweda LI. Declines in mitochondrial respiration during cardiac reperfusion: Age-dependent inactivation of alpha-ketoglutarate dehydrogenase. Proc Natl Acad Sci USA 1999; 96: 6689–6693
- Sadek HA, Humphries KM, Szweda PA, Szweda LI. Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion. Arch Biochem Biophys 2002; 406: 222–228
- Schapira AH. Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia. Biochim Biophys Acta 1999; 1410: 159–170
- Yarian CS, Toroser D, Sohal RS. Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice. Mech Ageing Dev 2006; 127: 79–84
- Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002; 4: 674–680
- Bota DA, Van Remmen H, Davies KJ. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett 2002; 532: 103–106
- Bota DA, Ngo JK, Davies KJ. Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic Biol Med 2005; 38: 665–677
- Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell 2005; 120: 483–495
- Harman D. Aging: A theory based on free radical and radiation chemistry. J Gerontol 1956; 11: 298–300
- Beckman KB, Ames BN. Oxidative decay of DMA. J Biol Chem 1997; 272: 19633–19636
- Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272: 20313–20316
- Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991; 11: 81–128
- Barrett WC, DeGnore JP, Keng YF, Zhang ZY, Yim MB, Chock PB. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem 1999; 274: 34543–34546
- Thomas JA, Poland B, Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 1995; 319: 1–9
- Thomas JA, Mallis RJ. Aging and oxidation of reactive protein sulfhydryls. Exp Gerontol 2001; 36: 1519–1526
- Tretter L, Adam-Vizi V. Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J Neurosci 2000; 20: 8972–8979