Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondrial

Biochemistry

Volumn 45, Issue 1, 2006, Pages 241-248

  Sharpley, Mark S ^a   Shannon, Richard J ^a   Draghi, Federica ^a   Hirst, Judy ^a  

^a WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; CHEMICAL ACTIVATION; ENERGY DISSIPATION; ENZYMES; PHOSPHOLIPIDS; STRUCTURAL ANALYSIS; SUBSTRATES;

BOVINE MITOCHONDRIAL; CARDIOLIPIN; ENERGY TRANSDUCING; NADH; PHOSPHATIDYLCHOLINE (PC);

DRUG INTERACTIONS;

BUFFER; CARDIOLIPIN; FLAVINE MONONUCLEOTIDE; IRON; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SULFUR; UBIQUINONE;

ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; COW; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBUNIT; HEART MITOCHONDRION; HYDROPHOBICITY; LIPID SOLUBILITY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION;

ANIMALS; CARDIOLIPINS; CATALYSIS; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, THIN LAYER; ELECTRON TRANSPORT COMPLEX I; HYDROPHOBICITY; MITOCHONDRIA; NAD; OXIDATION-REDUCTION; OXIDOREDUCTASES; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLETHANOLAMINES; PHOSPHOLIPIDS; SOLUBILITY; UBIQUINONE;

ANIMALIA; BOVINAE;

EID: 30144445462     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051809x     Document Type: Article

References (64)

1. Saraste, M. (1999) Oxidative phosphorylation at the fin de siècle, Science 283, 1488-1493.
2. Schultz, B. E., and Chan, S. I. (2001) Structures and proton-pumping strategies of mitochondrial respiratory enzymes, Annu. Rev. Biophys. Biomol. Struct. 30, 23-65.
3. Wikström, M. (1984) Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone, FEBS Lett. 169, 300-304.
4. Turrens, J. F., and Boveris, A. (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria, Biochem. J. 191, 421-427.
5. Smeitink, J., van den Heuvel, L., and DiMauro, S. (2001) The genetics and pathology of oxidative phosphorylation, Nat. Rev. Genet. 2, 342-352.
6. Walker, J. E. (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains, Q. Rev. Biophys. 25, 253-324.
7. 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.
8. Carroll, J., Fearnley, I. M., Shannon, R. J., Hirst, J., and Walker, J. E. (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria, Mol. Cell. Proteomics 2, 117-126.
9. Guénebaut, V., Schutt, A., Weiss, H., Leonard, K., and Friedrich, T. (1998) Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I), J. Mol. Biol. 276, 105-112.
10. Hinchliffe, P., and Sazanov, L. A. (2005) Organization of iron-sulfur clusters in respiratory complex I, Science 309, 771-774.
11. Hirst, J. (2005) Energy transduction by respiratory complex I-an evaluation of current knowledge, Biochem. Soc. Trans. 525-529.
12. Ohnishi, T. (1998) Iron-sulfur clusters/semiquinones in complex I, Biochim. Biophys. Acta 1364, 186-206.
13. Hellwig, P., Scheide, D., Bungert, S., Mäntele, W., and Friedrich, T. (2000) FT-IR spectroscopic characterization of NADH: ubiquinone oxidoreductase (complex I) from Escherichia coli: oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain, Biochemistry 39, 10884-10891.
14. Spehr, V., Schutt, A., Scheide, D., Guénebaut, V., and Friedrich, T. (1999) Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I), Biochemistry 38, 16261-16267.
15. Kerscher, S., Dröse, S., Zwicker, K., Zickermann, V., and Brandt, U. (2002) Yarrowia lipolytica, a yeast genetic system to study mitochondrial complex I, Biochim. Biophys. Acta 1555, 83-91.
16. Hatefi, Y., Haavik, A. G., and Griffiths, D. E. (1962) Studies on the electron-transfer system, J. Biol. Chem. 237, 1676-1680.
17. Walker, J. E., Skehel, J. M., and Buchanan, S. K. (1995) Structural analysis of NADH:ubiquinone oxidoreductase from bovine heart mitochondria, Methods Enzymol. 260, 14-34.
18. Finel, M., Skehel, J. M., Albracht, S. P. J., Fearnley, I. M., and Walker, J. E. (1992) Resolution of NADH-ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme, Biochemistry 31, 11425-11434.
19. 0-ATPase and complex I from bovine heart mitochondria, Biochem. J. 318, 343-349.
20. Sazanov, L. A., Peak-Chew, S. Y., Fearnley, I. M., and Walker, J. E. (2000) Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme, Biochemistry 39, 7229-7235.
21. Okun, J. G., Zickermann, V., Zwicker, K., Schägger, H., and Brandt, U. (2000) Binding of detergents and inhibitors to bovine complex I-a novel purification procedure for bovine complex I retaining full inhibitor sensitivity, Biochim. Biophys. Acta 1459, 77-87.
22. Smith, A. L. (1967) Preparation, properties and conditions for assay of mitochondria: slaughterhouse material, small scale, Methods Enzymol. 10, 81-86.
23. Darley-Usmar, V. M., Capaldi, R. A., Takamiya, S., Millett, F., Wilson, M. T., Malatesta, F., and Sarti, P. (1987) in Mitochondria, A Practical Approach (Darley-Usmar, V. M., Rickwood, D., and Wilson, M. T., Eds.) pp 143-144, Oxford University Press, Oxford.
24. Burch, H. B. (1957) Fluorimetric assay of FAD, FMN, and riboflavin, Methods Enzymol. 3, 960-962.
25. Gliszczyńska-Świgło, A., and Koziołowa, A. (2000) Chromatographic determination of riboflavin and its derivatives in food, J. Chromatogr. A 881, 285-297.
26. Doeg, K. A., and Ziegler, D. M. (1962) Simplified methods for the estimation of iron in mitochondria and submitochondrial fractions, Arch. Biochem. Biophys. 97, 37-40.
27. Takada, M., Ikenoya, S., Yuzuriha, T., and Katayama, K. (1982) Studies on reduced and oxidized coenzyme Q (ubiquinones), Biochim. Biophys. Acta 679, 308-314.
28. Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification, Can. J. Biochem. Physiol. 37, 911-917.
29. Skipski, V. P., Peterson, R. F., and Barclay, M. (1964) Quantitative analysis of phospholipids by thin-layer chromatography, Biochem. J. 90, 374-378.
30. Gomez, B., and Robinson, N. C. (1999) Quantitative determination of cardiolipin in mitochondrial electron transferring complexes by silicic acid high-performance liquid chromatography, Anal. Biochem. 267, 212-216.
31. Schlame, M., Brody, S., and Hosteller, K. Y. (1993) Mitochondrial cardiolipin in diverse eukaryotes, Eur. J. Biochem. 212, 727-735.
32. Grit, M., Crommelin, D. J. A., and Lang, J. (1991) Determination of phosphatidylcholine, phosphatidylglycerol and their lyso forms from liposome dispersions by high-performance liquid chromatography using high-sensitivity refractive index detection, J. Chromatogr, A 585, 239-246.
33. Schlame, M., Beyer, K., Hayer-Hartl, M., and Klingenberg, M. (1991) Molecular species of cardiolipin in relation to other mitochondrial phospholipids, Eur. J. Biochem. 199, 459-466.
34. Daum, G. (1985) Lipids of mitochondria, Biochim. Biophys. Acta 822, 1-42.
35. Fleischer, S., Rouser, G., Fleischer, B., Casu, A., and Kritchevsky, G. (1967) Lipid composition of mitochondria from bovine heart, liver, and kidney, J. Lipid Res. 8, 170-180.
36. Holub, B. J., and Kuksis, A. (1978) Metabolism of molecular species of diacylglycerophospholipids, Adv. Lipid Res. 16, 1-125.
37. McHowat, J., Jones, J. H., and Creer, M. H. (1996) Quantitation of individual phospholipid molecular species by UV absorption measurements, J. Lipid Res. 37, 2450-2460.
38. Rao, N. A., Felton, S. P., Huennekens, F. M., and Mackler, B. (1963) Flavin mononucleotide: the coenzyme of reduced diphosphopyridine nucleotide dehydrogenase, J. Biol. Chem. 238, 449-455.
39. Albracht, S. P. J., van der Linden, E., and Faber, B. W. (2003) Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (complex I) and related enzymes. Consequences for the number of prosthetic groups, Biochim. Biophys. Acta 1557, 41-49.
40. Sinegina, L., Wikström, M., Verkhovsky, M. I., and Verkhovskaya, M. L. (2005) Activation of isolated NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters, Biochemistry 44, 8500-8506.
41. Ohnishi, T., Leigh, J. S., Ragan, C. I., and Racker, E. (1974) Low-temperature electron paramagnetic resonance studies of iron-sulfur centers in cardiac NADH dehydrogenase, Biochem. Biophys. Res. Commun. 56, 775-782.
42. Dröse, S., Zwicker, K., and Brandt, U. (2002) Full recovery of the NADH:ubiquinone activity of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids, Biochim. Biophys. Acta 1556, 65-72.
43. Ragan, C. I. (1976) NADH-ubiquinone oxidoreductase, Biochim. Biophys. Acta 456, 249-290.
44. Dowhan, W., Mileykovskaya, E., and Bogdanov, M. (2004) Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches, Biochim. Biophys. Acta 1666, 19-39.
45. Lee, A. G. (2004) How lipids affect the activities of integral membrane proteins, Biochim. Biophys. Acta 1666, 62-87.
46. Schlame, M., Rua, D., and Greenberg, M. L. (2000) The biosynthesis and functional role of cardiolipin, Prog. Lipid Res. 39, 257-288.
47. Palsdottir, H., and Hunte, C. (2004) Lipids in membrane protein structures, Biochim. Biophys. Acta 1666, 2-18.
48. Fyfe, P. K., McAuley, K. E., Roszak, A. W., Isaacs, N. W., Cogdell, R. J., and Jones, M. R. (2001) Probing the interface between membrane proteins and membrane lipids by X-ray crystallography, Trends Biochem. Sci. 26, 106-112.
49. Robinson, N. C. (1982) Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidase, Biochemistry 21, 184-188.
50. 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure, Biochemistry 38, 14966-14972.
51. 1 complex, Eur. J. Biochem. 190, 123-130.
52. Hayer-Hartl, M., Schägger, H., von Jagow, G., and Beyer, K. (1992) Interactions of phospholipids with the mitochondrial cytochrome c reductase studied by spin-label ESR and NMR spectroscopy, Eur. J. Biochem. 209, 423-430.
53. 1 complex structure, EMBO J. 20, 6591-6600.
54. Rinyu, L., Martin, E. W., Takahashi, E., Maroti, P., and Wraight, C. A. (2004) Modulation of the free energy of the primary quinone acceptor (QA) in reaction centers from Rhodobacter sphaeroides: contributions from the protein and protein-lipid(cardiolipin) interactions, Biochim. Biophys. Acta 1655, 93-101.
55. Paradies, G., Petrosillo, G., Pistolese, M., and Ruggiero, F. M. (2002) Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage, Gene 286, 135-141.
56. Ragan, C. I., and Racker, E. (1973) Resolution and reconstitution of the mitochondrial electron transport system, J. Biol. Chem. 248, 6876-6884.
57. Heron, C., Corina, D., and Ragan, C. I. (1977) The phospholipid annulus of mitochondrial NADH-ubiquinone reductase, FEBS Lett. 79, 399-403.
58. Fry, M., and Green, D. E. (1981) Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain, J. Biol. Chem. 256, 1874-1880.
59. Poore, V. M., and Ragan, C. I. (1982) A spin label study of the lipid boundary layer of mitochondrial NADH-ubiquinone oxidoreductase, Biochim. Biophys. Acta 693, 105-112.
60. Ragan, C. I. (1978) The role of phospholipids in the reduction of ubiquinone analogues by the mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone oxidoreductase complex, Biochem. J. 172, 539-547.
61. Sazanov, L. A., Carroll, J., Holt, P., Toime, L., and Fearnley, I. M. (2003) A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I), J. Biol. Chem. 278, 19483-19491.
62. Rich, P. R., and Harper, R. (1990) Partition coefficients of quinones and hydroquinones and their relation to biochemical reactivity, FEBS Lett. 269, 139-144.
63. Degli Esposti, M., Ngo, A., McMullen, G. L., Ghelli, A., Sparta, F., Benelli, B., Ratta, M., and Linnane, A. W. (1996) The specificity of mitochondrial complex I for ubiquinones, Biochem. J. 313, 327-334.
64. Lenaz, G. (1998) Quinone specificity of complex I, Biochim. Biophys. Acta 1364, 207-221.