α-Ketoglutarate dehydrogenase: A mitochondrial redox sensor

References

• Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002;82:47–95.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Rhee SG. Redox signaling: hydrogen peroxide as intracellular messenger. Exp Mol Med 1999;31:53–59.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Forman HJ, Maiorino M, Ursini F. Signaling functions of reactive oxygen species. Biochemistry ;49:835–842.
   Google Scholar
• Yap LP, Garcia JV, Han D, Cadenas E. The energy-redox axis in aging and age-related neurodegeneration. Adv Drug Deliv Rev 2009;61:1283–1298.
   Google Scholar
• Ambrosio G, Tritto I, Chiariello M. The role of oxygen free radicals in preconditioning. J Mol Cell Cardiol 1995;27: 1035–1039.
   PubMed Web of Science ®Google Scholar
• Baines CP, Goto M, Downey JM. Oxygen radicals released during ischemic preconditioning contribute to cardioprotection in the rabbit myocardium. J Mol Cell Cardiol 1997;29: 207–216.
   PubMed Web of Science ®Google Scholar
• da Silva MM, Sartori A, Belisle E, Kowaltowski AJ. Ischemic preconditioning inhibits mitochondrial respiration, increases H2O2 release, and enhances K+ transport. Am J Physiol Heart Circ Physiol 2003;285:154–162.
   Google Scholar
• Halestrap AP, Clarke SJ, Khaliulin I. The role of mitochondria in protection of the heart by preconditioning. Biochim Biophys Acta 2007;1767:1007–1031.
   PubMed Web of Science ®Google Scholar
• Kevin LG, Camara AK, Riess ML, Novalija E, Stowe DF. Ischemic preconditioning alters real-time measure of O2 radicals in intact hearts with ischemia and reperfusion. Am J Physiol Heart Circ Physiol 2003;284:566–574.
   PubMed Web of Science ®Google Scholar
• Novalija E, Hogg N, Kevin LG, Camara AK, Stowe DF. Ischemic preconditioning: triggering role of nitric oxide-derived oxidants in isolated hearts. J Cardiovasc Pharmacol 2003;42:593–600.
   Google Scholar
• Tritto I, D'Andrea D, Eramo N, Scognamiglio A, De Simone C, Violante A, Esposito A, Chiariello M, Ambrosio G. Oxygen radicals can induce preconditioning in rabbit hearts. Circ Res 1997;80:743–748.
   PubMed Web of Science ®Google Scholar
• Yaguchi Y, Satoh H, Wakahara N, Katoh H, Uehara A, Terada H, Fujise Y, Hayashi H. Protective effects of hydrogen peroxide against ischemia/reperfusion injury in perfused rat hearts. Circ J 2003;67:253–258.
   Google Scholar
• Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 2000;29: 222–230.
   PubMed Web of Science ®Google Scholar
• Chance B, Williams GR. The respiratory chain and oxidaive phosphorylation. Adv Enzymol Relat Subj Biochem 1956;17: 65–134.
   PubMedGoogle Scholar
• Nulton-Persson AC, Szweda LI. Modulation of mitochondrial function by hydrogen peroxide. J Biol Chem 2001; 276:23357–23361.
   PubMed Web of Science ®Google Scholar
• Rokutan K, Kawai K, Asada K. Inactivation of 2-oxoglutarate dehydrogenase in rat liver mitochondria by its substrate and t-butyl hydroperoxide. J Biochem 1987;101: 415–422.
   Google Scholar
• Applegate MA, Humphries KM, Szweda LI. Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid. Biochemistry 2008;47:473–478.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Humphries KM, Yoo Y, Szweda LI. Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal. Biochemistry 1998;37:552–557.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Korotchkina LG, Yang H, Tirosh O, Packer L, Patel MS. Protection by thiols of the mitochondrial complexes from 4-hydroxy-2-nonenal. Free Radic Biol Med 2001;30: 992–999.
   PubMed Web of Science ®Google Scholar
• Cooney GJ, Taegtmeyer H, Newsholme EA. Tricarboxylic acid cycle flux and enzyme activities in the isolated working rat heart. Biochem J 1981;200:701–703.
   PubMed Web of Science ®Google Scholar
• Moreno-Sanchez R, Hogue BA, Hansford RG. Influence of NAD-linked dehydrogenase activity on flux through oxidative phosphorylation. Biochem J 1990;268:421–428.
   Google Scholar
• Gibson GE, Park LC, Sheu KF, Blass JP, Calingasan NY. The alpha-ketoglutarate dehydrogenase complex in neurodegeneration. Neurochem Int 2000;36:97–112.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Lundberg KC, Szweda LI. Preconditioning prevents loss in mitochondrial function and release of cytochrome c during prolonged cardiac ischemia/reperfusion. Arch Biochem Biophys 2006;453:130–134.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Beal MF. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann Neurol 1995;38:357–366.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Reed LJ. Multienzyme complexes. Acc Chem Res 1974; 7:40–46.
   Web of Science ®Google Scholar
• Waskiewicz DE, Hammes GG. Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation. Biochemistry 1984;23: 3136–3143.
   Google Scholar
• Perham RN. Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 1991;30: 8501–8512.
   Google Scholar
• Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991;11:81–128.
   PubMed Web of Science ®Google Scholar
• Bulteau AL, Ikeda-Saito M, Szweda LI. Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry 2003;42:14846–14855.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Fukushima T, Decker RV, Anderson WM, Spivey HO. Substrate channeling of NADH and binding of dehydrogenases to complex I. J Biol Chem 1989;264:16483–16488.
   Google Scholar
• Maas E, Bisswanger H. Localization of the alpha-oxoacid dehydrogenase multienzyme complexes within the mitochondrion. FEBS Lett 1990;277:189–190.
   Google Scholar
• Porpaczy Z, Sumegi B, Alkonyi I. Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase. J Biol Chem 1987;262:9509–9514.
   PubMed Web of Science ®Google Scholar
• Sumegi B, Srere PA. Complex I binds several mitochondrial NAD-coupled dehydrogenases. J Biol Chem 1984; 259:15040–15045.
   PubMedGoogle Scholar
• Huang HM, Ou HC, Xu H, Chen HL, Fowler C, Gibson GE. Inhibition of alpha-ketoglutarate dehydrogenase complex promotes cytochrome c release from mitochondria, caspase-3 activation, and necrotic cell death. J Neurosci Res 2003;74:309–317.
   Google Scholar
• Bunik V, Raddatz G, Lemaire S, Meyer Y, Jacquot JP, Bisswanger H. Interaction of thioredoxins with target proteins: role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes. Protein Sci 1999;8:65–74.
   Google Scholar
• Bunik VI. 2-Oxo acid dehydrogenase complexes in redox regulation. Eur J Biochem 2003;270:1036–1042.
   PubMedGoogle Scholar
• Bunik V, Follmann H, Bisswanger H. Activation of mitochondrial 2-oxoacid dehydrogenases by thioredoxin. Biol Chem 1997;378:1125–1130.
   PubMedGoogle Scholar
• Bunik V, Follmann H. Thioredoxin reduction dependent on alpha-ketoacid oxidation by alpha-ketoacid dehydrogenase complexes. FEBS Lett 1993;336:197–200.
   Google Scholar
• Cussiol JR, Alegria TG, Szweda LI, Netto LE. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J Biol Chem 2010;285:21943–21950.
   PubMed Web of Science ®Google Scholar
• Shi Q, Chen HL, Xu H, Gibson GE. Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity. J Biol Chem 2005;280:10888–10896.
   Google Scholar
• Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 2002;295: 1073–1077.
   PubMed Web of Science ®Google Scholar
• Carothers DJ, Pons G, Patel MS. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch Biochem Biophys 1989;268:409–425.
   PubMed Web of Science ®Google Scholar
• Sandalova T, Zhong L, Lindqvist Y, Holmgren A, Schneider G. Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme. Proc Natl Acad Sci USA 2001;98:9533–9538.
   PubMed Web of Science ®Google Scholar
• Williams CH, Jr, Arscott LD, Schulz GE. Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase. Proc Natl Acad Sci USA 1982;79:2199–2201.
   PubMed Web of Science ®Google Scholar
• Babady NE, Pang YP, Elpeleg O, Isaya G. Cryptic proteolytic activity of dihydrolipoamide dehydrogenase. Proc Natl Acad Sci USA 2007;104:6158–6163.
   Google Scholar
• Gilbert HF. Thiol/disulfide exchange equilibria and disulfide bond stability. Method Enzymol 1995;251:8–28.
   PubMed Web of Science ®Google Scholar
• Klatt P, Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 2000;267:4928–4944.
   PubMedGoogle Scholar
• Dalle-Donne I, Rossi R, Giustarini D, Colombo R, Milzani A. S-glutathionylation in protein redox regulation. Free Radic Biol Med 2007;43:883–898.
   PubMed Web of Science ®Google Scholar
• Gallogly MM, Mieyal JJ. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol 2007;7:381–391.
   PubMed Web of Science ®Google Scholar
• Hurd TR, Filipovska A, Costa NJ, Dahm CC, Murphy MP. Disulphide formation on mitochondrial protein thiols. Biochem Soc Trans 2005;33:1390–1393.
   Google Scholar
• Ambrus A, Tretter L, Adam-Vizi V. Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid. J Neurochem 2009;109 (Suppl 1):222–229.
   Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Tretter L, Adam-Vizi V. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J Neurosci 2004;24:7771–7778.
   PubMed Web of Science ®Google Scholar
• Suzuki K, Reed LJ. Lipoamidase. J Biol Chem 1963;238: 4021–4025.
   Google Scholar
• Oizumi J, Hayakawa K. Lipoamidase is a multiple hydrolase. Biochem J 1990;271:45–49.
   Google Scholar
• Feng D, Witkowski A, Smith S. Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death. J Biol Chem 2009;284:11436–11445.
   Google Scholar
• Cicchillo RM, Iwig DF, Jones AD, Nesbitt NM, Baleanu-Gogonea C, Souder MG, Tu L, Booker SJ. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry 2004;43: 6378–6386.
   PubMedGoogle Scholar
• Miller JR, Busby RW, Jordan SW, Cheek J, Henshaw TF, Ashley GW, Broderick JB, Cronan JE, Jr, Marletta MA. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 2000;39:15166–15178.
   PubMedGoogle Scholar
• Morikawa T, Yasuno R, Wada H. Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria. FEBS Lett 2001;498:16–21.
   PubMed Web of Science ®Google Scholar
• Wada H, Shintani D, Ohlrogge J. Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production. Proc Natl Acad Sci USA 1997;94:1591–1596.
   PubMed Web of Science ®Google Scholar
• Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol 2003;10:1293–1302.
   PubMedGoogle Scholar