2-Oxo acid dehydrogenase complexes in redox regulation: Role of the lipoate residues and thioredoxin

European Journal of Biochemistry

Volumn 270, Issue 6, 2003, Pages 1036-1042

  Bunik, Victoria I ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

2 oxo acid dehydrogenase complex; Dihydrolipoate; Radical species; Redox state; Thioredoxin

Indexed keywords

2 OXOACID DEHYDROGENASE; COENZYME A; DIHYDROLIPOATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXOGLUTARATE DEHYDROGENASE; PEROXIDASE; PYRUVATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOCTIC ACID; THIOREDOXIN;

CHEMICAL REACTION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE; MAMMAL; METABOLIC REGULATION; MITOCHONDRION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SHORT SURVEY;

3-METHYL-2-OXOBUTANOATE DEHYDROGENASE (LIPOAMIDE); DISULFIDES; KETONE OXIDOREDUCTASES; MULTIENZYME COMPLEXES; NAD; OXIDATION-REDUCTION; SULFHYDRYL COMPOUNDS; SUPEROXIDES; THIOCTIC ACID; THIOREDOXIN;

MAMMALIA;

EID: 0037352050     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03470.x     Document Type: Short Survey

References (61)

1. Gilbert, H. (1984) Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol. 107, 330-351.
2. +) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. J. Bacteriol. 181, 2351-2357.
3. Pani, G., Colavitti, R., Borrello, S. & Galeotti, T. (2000) Redox regulation of lymphocyte signalling. JUBMB Life 49, 381-389.
4. Rusnak, F. & Reiter, T. (2000) Sensing electrons: protein phosphatase redox regulation. Trends Biochem. Sci. 25, 527-529.
5. Danon, A. (2002) Redox reactions of regulatory proteins: do kinetics promote specificity? Trends Biochem. Sci. 27, 197-203.
6. Mieyal, J.J., Srinivasan, U., Starke, D.W., Gravina, S.A. & Mieyal, P.A. (1995) Glutathionyl specificity of thioltransferases: mechanistic and physiological implications. In Biothiols in Health and Disease (Packer, L. & Cadenas, E., eds), pp. 305-372. Marcel Dekker, Inc., New York, USA.
7. Klatt, P. & Lamas, S. (2000) Regulation of protein function by S-glutathionylation in response to oxidative and nitrosative stress. Eur. J. Biochem. 267, 4928-4944.
8. Cross, A.R. & Jones, O.T.G. (1991) Enzymic mechanisms of superoxide production. Biochim. Biophys. Acta 1057, 281-298.
9. Romero, F.J., Ordonez, I., Arduini, A. & Cadenas, E. (1992) The reactivity of thiols and disulfides with different redox states of myoglobin. J. Biol. Chem. 267, 1680-1688.
10. Winterbourn, C.C. & Metodieva, D. (1994) The reaction of superoxide with reduced glutathione. Arch. Biochem. Biophys. 314, 284-290.
11. Nordberg, J. & Arner, E.S.J. (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Rad. Biol. Med. 31, 1287-1312.
12. Ullrich, V. & Bachschmid, M. (2000) Superoxide as a messenger of endotelial function. Biochem. Biophys. Res. Communs. 278, 1-8.
13. Aslund, F., Zheng, M., Beckwith, J. & Storz, G. (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc. Natl Acad. Sci. USA 96, 6161-6165.
14. Schulz, J.B., Lindenau, J., Seyfried, J. & Dichgans, J. (2000) Glutathione, oxidative stress and neurodegeneration. Eur. J. Biochem. 207, 4904-4911.
15. Sastre, J., Pallardo, F.V. & Vina, J. (2000) Mitochondrial oxidative stress plays a key role in aging and apoptosis. JUBMB Life 49, 427-435.
16. Skulachev, V.P. (2001) NAD(P)+ decomposition and antioxidant defense of the cell. FEBS Left. 492, 1-3.
17. + metabolism. FEBS Lett. 492, 4-8.
18. Massey, V. (1963) Lipoyl dehydrogenase. Enzymes 7, 275-306.
19. de Kok, A. & van Berkel, W.J.H. (1996) Lipoamide dehydrogenase. In α-Keto Acid Dehydrogenase Complexes (Patel, M.S., Roche, T.E. & Harris, R.A., eds), pp. 53-70. Birkhaeuser Verlag, Basel-Boston-Berlin.
20. Snoep, J.L., de Graft, M.R., Westphal, A.H., de Kok, A., de Mattos, M.J.T. & Neijssel, O.M. (1993) Differences in sensitivity to NADH of purified pyruvate dehydrogenase complexes of Enterococcus faecalis, Lactococcas lactis, Azotobacter vinelandii and Escherichia coli: implications for their activity in vivo. FEMS Lett. 114, 279-284.
21. Skrede, S., Bremer, J. & Elsjarn, L. (1965) The effect of disulfides on mitochondrial oxidation. Biochem. J. 95, 838-884.
22. Skrede, S. (1968) The mechanism of disulfide reduction by mitochondria. Biochem. J. 108, 693-699.
23. Biewenga, G.P., Haenen, G.R. & Bast, A. (1997) The pharmacology of the antioxidant lipoic acid. Gen. Pharmacol. 29, 315-331.
24. Packer, L., Witt, E.H. & Tritschler, H.J. (1995) Alpha-lipoic acid as a biological antioxidant. Free Rad. Biol. Med. 19, 227-250.
25. Scott, B.C., Aruoma, O.I., Evans, P.J., O'Neill, C., Van der Vliet, A., Cross, C.E., Tritschler, H. & Halliwell, B. (1994) Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation. Free Rad. Res. 20, 119-133.
26. Suzuki, Y.J., Mizuno, M., Tritschler, H.J. & Packer, L. (1995) Redox regulation of NF-kappa B DNA binding activity by dihydrolipoate. Biochem. Mol. Biol. Internat. 36, 241-246.
27. Holmgren, A. (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632.
28. Masutani, H. & Yodoi, J. (2002) Thioredoxin. Overview. Methods Enzymol. 347, 279-286.
29. Asmus, K.-D. (1990) Sulfur-centered free radicals. Methods Enzymol. 186, 168-180.
30. de Kok, A., Hengeveld, A.F., Martin, A. & Westphal, A.H. (1998) The pyruvate dehydrogenase complex from Gram-negative bacteria. Biochim. Biophys. Acta 1385, 353-366.
31. De la Sierra, I.L., Pernot, L., Prange, T., Saludjian, P., Schiltz, M., Fourme, R. & Padron, G. (1997) Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. J. Mol. Biol. 269, 129-141.
32. Perham, R.N. (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Ann. Rev. Biochem. 69, 961-1004.
33. Berg, A. & de Kok, A. (1997) 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain. Biol. Chem. 378, 617-634.
34. Hackert, M.L., Oliver, R.M. & Reed, L.J. (1983) A computer model analysis of the active-site coupling mechanism in the pyruvate dehydrogenase complex of Escherichia coli. Proc. Natl Acad. Sci. USA 80, 2907-2911.
35. Danson, M.J., Ferscht, A.R. & Perham, R.N. (1978) Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli: mechanism for rate enhancement in a multimeric structure. Proc. Natl Acad. Sci. USA 75, 5386-5390.
36. Collins, J.H. & Reed, L.J. (1977) Acyl group and electron pair relay system: a network of interacting lipoyl moieties in the pyruvate and α-ketoglutarate dehydrogenase complexes from Escherichia coli. Proc. Natl. Acad. Sci. USA 74, 4223-4227.
37. Guest, J.R., Ali, S.T., Artymiuk, P., Ford, G.C., Green, J. & Russel, G.C. (1990) Site-directed mutagenesis of dihydrolipoamide acetyltransferase and post-translational modification of its lipoyl domains. In Biochemistry and Physiology of Thiamin Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds), pp. 176-193. Chemic, Weinheim, Germany.
38. Guest, J.R., Attwood, M.M., Machado, R.S., Matqi, K.Y., Shaw, J.E. & Turner, S.L. (1997) Enzymological and physiological consequences of restructuring the lipoyl domain content of the pyruvate dehydrogenase complex of Escherichia coli. Microbiology 143, 457-466.
39. Dave, E., Guest, J.R. & Attwood, M.M. (1995) Metabolic engineering in Escherichia coli: lowering the lipoyl domain content of the pyruvate dehydrogenase complex adversely affects the growth rate and yield. Microbiology 141, 1839-1849.
40. Bunik, V.I., Buneeva, O.A. & Gomazkova, V.S. (1990) Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH. FEBS Lett. 269, 252-254.
41. Bunik, V. (2000) Increased catalytic performance of the 2-oxo acid dehydrogenase complexes in the presence of thioredoxin, a thioldisulfide oxidoreductase. J. Molec. Catalysis B: Enzymatic 8, 165-174.
42. Bunik, V. & Sievers, C. (2002) Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 269, 5004-5015.
43. Raddatz, G., Kruft, V. & Bunik, V. (2000) Structural determinants for the efficient and specific interaction of thioredoxin with 2-oxo acid dehydrogenase complexes. Appl. Biochem. Biotechnol. 88, 77-96.
44. Matthews, R.G. & Williams, C.H. Jr (1976) Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. J. Biol. Chem. 251, 3956-3964.
45. Russel, R.R. III & Taegtmcyer, H. (1992) Coenzyme A sequestration in rat hearts oxidising ketone bodies. J. Clin. Invest. 89, 968-973.
46. Gibson, G.E., Park, L.C.H., Sheu, K.-F.R., Blass, J.P. & Calingasan, N.Y. (2000) α-Ketoglutarate dehydrogenase complex in neurodegeneration. Neurochem. Int. 36, 97-112.
47. Bunik, V., Raddatz, G., Lemaire, S., Meyer, Y., Jacquot, J.-P. & Bisswanger, H. (1999) Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxo acid dehydrogenase complexes. Prot. Sci. 8, 65-74.
48. Bunik, V. & Follmann, F. (1993) Thioredoxin reduction dependent on α-keto acid oxidation by α-keto acid dehydrogenase complexes. FEBS Lett. 336, 197-200.
49. Bunik, V., Shoubnikova, A., Loeffelhardt, S., Bisswanger, H., Borbe, H.O. & Follmann, H. (1995) Using lipoate enantiomers and thioredoxin to study mechanism 2-oxo acid-dependent dihydrolipoate production by the 2-oxo acid dehydrogenase complexes. FEBS Lett. 371, 167-170.
50. Bryk, R., Lima, C.D., Erdjument-Bromage, H., Tempst, P. & Nathan, C. (2002) Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295, 1073-1077.
51. Bodenstein-Lang, J., Buch, A. & Follmann, H. (1989) Animal and plant mitochondria contain specific thioredoxins. FEBS Lett. 258, 22-26.
52. Bunik, V., Follmann, H. & Bisswanger, H. (1997) Activation of mitochondrial 2-oxo acid dehydrogenases by thioredoxin. Biol. Chem. 378, 1125-1130.
53. Janin, J. (1997) Kinetics of protein-protein recognition. Proteins 28, 153-161.
54. Hanine, L.C., El Conte, D., Jacquot, J.-P. & Houee-Levin, C. (2000) Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme: a pulse radiolysis study. Biochemistry 39, 9295-9301.
55. Saez, G., Thornalley, P.J., Hill, H.A.O., Hems, R. & Bannister, J.V. (1982) The production of free radicals during the autoxidation of cysteine and their effect on isolated rat hepatocytes. Biochim. Biophys. Acta 719, 24-31.
56. Harman, L.S., Mottley, C. & Mason, R.P. (1984) Free radical metabolites of L-cysteine oxidation. J. Biol. Chem. 259, 5606-5561.
57. Watabe, S., Hiroi, T., Yamamoto, Y., Fujioka, Y., Hagesawa, H., Yago, N. & Takahashi, S.Y. (1997) SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria. Eur. J. Biochem. 249, 52-60.
58. Chen, Y., Cai, J., Murphy, T.J. & Jones, D.P. (2002) Over-expressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J. Biol. Chem. 277, 33242-33248.
59. Cabiscol, E., Piulats, E., Echave, P., Herrero, E. & Ros, J. (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J. Biol. Chem. 275, 27393-27398.
60. Rokutan, K., Kawai, K. & Asada, K. (1987) Inactivation of 2-oxoglutarate dehydrogenase in rat liver mitochondrial by its substrate and t-butyl hydroperoxide. J. Biochem. 101, 415-422.
61. Regnstrom, K., Sauge-Merle, S., Chen, K. & Burgess, B.K. (1999) In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds for promoter region DNA and ferredoxin I. Proc. Natl Acad. Sci. USA 96, 12389-12393.