Transhydrogenation reactions catalyzed by mitochondrial NADH-ubiquinone oxidoreductase (complex I)

Biochemistry

Volumn 46, Issue 49, 2007, Pages 14250-14258

  Yakovlev, Gregory ^a   Hirst, Judy ^a  

^a WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON TRANSPORT CHAIN; HYDRIDE TRANSFERS; MITOCHONDRIA; UBIQUINONE REDUCTION;

CATALYSIS; CELL MEMBRANES; ELECTRON TRANSPORT PROPERTIES; HYDRIDES; NUCLEOTIDES; OXIDATION;

ENZYMES;

OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UBIQUINONE OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROGENATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL;

ANIMALS; CATTLE; ELECTRON TRANSPORT COMPLEX I; HYDROGEN; MITOCHONDRIA, HEART; NAD; NADP;

EID: 37049000017     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7017915     Document Type: Article

References (53)

1. Walker, J. E. (1992) The NADH-ubiquinone oxidoreductase (complex I) of respiratory chains, Q. Rev. Biophys. 25, 253-324.
2. Yagi, T., and Matsuno-Yagi, A. (2003) The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked, Biochemistry 42, 2266-2274.
3. Hirst, J. (2005) Energy transduction by respiratory complex I - an evaluation of current knowledge, Biochem. Soc. Trans. 33, 525-529.
4. Sazanov, L. A. (2007) Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain, Biochemistry 46, 2275-2288.
5. Wikström, M. (1984) Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone, FEBS Lett. 169, 300-304.
6. Chance, B., and Hollunger, G. (1961) The interaction of energy and electron transfer reactions in mitochondria, J. Biol. Chem. 236, 1534-1543.
7. Chance, B., Lees, H., and Postgate, J. R. (1972) The meaning of "reversed electron flow" and "high energy electron" in biochemistry, Nature 238, 330-331.
8. Hatefi, Y., and Galante, Y. M. (1977) Dehydrogenase and transhydrogenase properties of the soluble NADH dehydrogenase of bovine heart mitochondria, Proc. Natl. Acad. Sci. U.S.A. 74, 846-850.
9. Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., and Parker, N. (2004) Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins, Free Rad. Biol. Med. 37, 755-767.
10. Kussmaul, L., and Hirst, J. (2006) The mechanism of superoxide production by NADH:ubiquinone oxidoreductase from bovine heart mitochondria, Proc. Natl. Acad. Sci. U.S.A. 103, 7607-7612.
11. Lambert, A. J., and Brand, M. D. (2004) Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane, Biochem. J. 382, 511-517.
12. Hoek, J. B., and Rydström, J. (1988) Physiological roles of nicotinamide nucleotide transhydrogenase, Biochem. J. 254, 1-10.
13. Jackson, J. B., White, S. A., Quirk, P. G., and Venning, J. D. (2002) The alternating site, binding change mechanism for proton translocation by transhydrogenase, Biochemistry 41, 4173-4185.
14. Jackson, J. B. (2003) Proton translocation by transhydrogenase, FEBS Lett. 545, 18-24.
15. Bücher, T., and Sies, H. (1976) Mitochondrial and cytosolic redox states in perfused rat liver: methods and problems in metabolic compartmentation, in Use of isolated liver cells and kidney tubules in metabolic studies (Tager, J. M., Söling, H. D., and Williamson, J. R., Eds.) pp 41-64, North-Holland Publishing Company, Amsterdam.
16. Tischler, M. E., Friedrichs, D., Coll, K., and Williamson, J. R. (1977) Pyridine nucleotide distributions and enzyme mass action ratios in hepatocytes from fed and starved rats, Arch. Biochem. Biophys. 184, 222-236.
17. Williamson, J. R., and Corkey, B. E. (1979) Assay of citric acid cycle intermediates and related compounds - update with tissue metabolite levels and intracellular distribution, Methods Enzymol. 55, 200-222.
18. Sies, H. (1982) Nicotinamide nucleotide compartmentation, in Metabolic compartmentation (Sies, H., Ed.) pp 205-231, Academic Press, London.
19. Nicholls, D. G., and Ferguson, S. J. (2002) Bioenergetics 3, Academic Press, London.
20. Minakami, S., Ringler, R. L., and Singer, T. P. (1962) Studies on the respiratory chain-linked dihydrodiphosphopyridine nucleotide dehydrogenase, J. Biol. Chem. 237, 569-576.
21. Minakami, S., Cremona, T., Ringler, R. L., and Singer, T. P. (1963) Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase, J. Biol. Chem. 238, 1529-1537.
22. Hatefi, Y., and Hanstein, W. G. (1973) Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondria, Biochemistry 12, 3515-3522.
23. Djavadi-Ohaniance, L., and Hatefi, Y. (1975) Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD, J. Biol. Chem. 250, 9397-9403.
24. Zakharova, N. V., Zharova, T. V., and Vinogradov, A. D. (1999) Kinetics of transhydrogenase reaction catalyzed by the mitochondrial NADH-ubiquinone oxidoreductase (complex I) imply more than one catalytic nucleotide-binding sites, FEBS Lett. 444, 211-216.
25. Zakharova, N. V. (2002) Kinetics of the transhydrogenase reaction catalyzed by mitochondrial NADH:ubiquinone oxidoreductase (complex I), Biochemistry (Mosc.) 67, 651-661.
26. Zakharova, N. V., and Zharova, T. V. (2002) Kinetic mechanism of mitochondrial NADH:ubiquinone oxidoreductase interaction with nucleotide substrates of the transhydrogenase reaction, Biochemistry (Mosc.) 67, 1395-1404.
27. Sharpley, M. S., Shannon, R. J., Draghi, F., and Hirst, J. (2006) Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria, Biochemistry 45, 241-248.
28. Sherwood, S., and Hirst, J. (2006) Investigation of the mechanism of proton translocation by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria: does the enzyme operate by a Q-cycle mechanism? Biochem. J. 400, 541-550.
29. Clark, W. M. (1960) Oxidation-reduction potentials of organic systems, The Williams and Wilkins Company, Baltimore.
30. Horecker, B. L., and Kornberg, A. (1948) The extinction coefficients of the reduced band of pyridine nucleotides, J. Biol. Chem. 175, 385-390.
31. Woenckhaus, C., and Jeck, R. (1987) Preparation and properties of NAD and NADP analogues, in Pyridine nucleotide coenzymes, chemical, biochemical and medical aspects (Dolphin, D., Poulson, R., and Avramović, O., Eds.) pp 449-568, John Wiley & Sons, Toronto.
32. van Kuilenburg, A. B. P., Elzinga, L., van den Berg, A. A., Slingerland, R. J., and van Gennip, A. H. (1994) A fast and novel assay of CTP synthase: evidence for hysteretic properties of the mammalian enzyme, Anticancer Res. 14, 411-416.
33. Anderson, B. M., and Kaplan, N. O. (1958) Enzymatic studies with analogues of diphosphopyridine nucleotide, J. Biol. Chem. 234, 1226-1232.
34. Keister, D. L., and Hemmes, R. B. (1966) Pyridine nucleotide transhydrogenase from Chromatium, J. Biol. Chem. 241, 2820-2825.
35. Stocchi, V., Cucchiarini, L., Canestrari, F., Piacentini, M. P., and Fornaini, G. (1987) A very fast ion-pair reversed-phase HPLC method for the separation of the most significant nucleotides and their degradation products in human red blood cells, Anal. Biochem. 167, 181-190.
36. Sazanov, L. A., and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus, Science 311, 1430-1436.
37. Sled, V. D., Rudnitzky, N. I., Hatefi, Y., and Ohnishi, T. (1994) Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I), Biochemistry 33, 10069-10075.
38. Briggs, G. E., and Haldane, J. B. S. (1925) A note on the kinetics of enzyme action, Biochem. J. 19, 338-339.
39. + with the mitochondrial NADH dehydrogenase, J. Biol. Chem. 256, 8318-8323.
40. Yamaguchi, M., Belogrudov, G. I., and Hatefi, Y. (1998) Mitochondrial NADH-ubiquinone oxidoreductase (complex I) - effects of substrates on the fragmentation of subunits by trypsin, J. Biol. Chem. 273, 8094-8098.
41. Abdrakhmanova, A., Zwicker, K., Kerscher, S., Zickermann, V., and Brandt, U. (2006) Tight binding of NADPH to the 39 kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex, Biochim. Biophys. Acta 1757, 1676-1682.
42. Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., and Walker, J. E. (2003) The nuclear encoded subunits of complex I from bovine heart mitochondria, Biochim. Biophys. Acta 1604, 135-150.
43. Zickermann, V., Zwicker, K., Tocilescu, M. A., Kerscher, S., and Brandt, U. (2007) Characterization of a subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (complex I) lacking the flavoprotein part of the N-module, Biochim. Biophys. Acta 1767, 393-400.
44. Albracht, S. P. J., Mariette, A., and de Jong, P. (1997) Bovine heart NADH:ubiquinone oxidoreductase is a monomer with eight iron sulfur clusters and two FMN groups, Biochim. Biophys. Acta 1318, 92-106.
45. Hatefi, Y., and Bearden, A. J. (1976) Electron paramagnetic resonance studies on the reduction of the components of complex I and transhydrogenase- inhibited complex I by NADH and NADPH, Biochem. Biophys. Res. Commun. 69, 1032-1038.
46. Zharova, T. V., and Vinogradov, A. D. (1997) A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) by ADP-ribose, Biochim. Biophys. Acta 1320, 256-264.
47. Vinogradov, A. D. (1993) Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH:ubiquinone reductase, J. Bioenerg. Biomembr. 25, 367-375.
48. Singh, A., Venning, J. D., Quirk, P. G., van Boxel, G. I., Rodrigues, D. J., White, S. A., and Jackson, J. B. (2003) Interactions between transhydrogenase and thio-nicotinamide analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation, J. Biol. Chem. 278, 33208-33216.
49. Fersht, A. R. (1998) Structure and mechanism in protein science, W. H. Freeman and Co., New York.
50. + reduction by mitochondrial complex I, Biochemistry (Mosc.) 56, 1181-1189.
51. Sled, V. D., and Vinogradov, A. D. (1993) Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexaammineruthenium (III), Biochim. Biophys. Acta 1141, 262-268.
52. Vogel, R., Wiesinger, H., Hamprecht, B., and Dringen, R. (1999) The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required, Neurosci. Lett. 275, 97-100.
53. Rydström, J. (2006) Mitochondrial NADPH, transhydrogenase and disease, Biochim. Biophys. Acta 1757, 721-726.