The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I

Biochemistry

Volumn 42, Issue 3, 2003, Pages 746-754

  Nakamaru Ogiso, Eiko ^a   Sakamoto, Kimitoshi ^b   Matsuno Yagi, Akemi ^a   Miyoshi, Hideto ^b   Yagi, Takao ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; ENZYMES; OXIDATION; RADIOACTIVITY;

BOVINE MITOCHONDRIAL COMPLEXES;

BIOCHEMISTRY;

(TRIFLUOROMETHYL)PHENYLDIAZIRINYLFENPYROXIMATE H 3; AMILORIDE DERIVATIVE; ENZYME INHIBITOR; FENPYROXIMATE; POTASSIUM FERRICYANIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME SUBUNIT; GEL ELECTROPHORESIS; ILLUMINATION; NONHUMAN; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTON SODIUM EXCHANGE; RADIOACTIVITY; ULTRAVIOLET RADIATION;

AMINO ACID SEQUENCE; ANIMALS; BENZOATES; CATTLE; MITOCHONDRIA, HEART; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NAD; NADP; PHOTOAFFINITY LABELS; PROTEIN SUBUNITS; PYRAZOLES; QUINONE REDUCTASES; SODIUM-HYDROGEN ANTIPORTER; SUBMITOCHONDRIAL PARTICLES;

BOVINAE;

EID: 0347295939     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0269660     Document Type: Article

References (75)

1. Scheffler, I. E. (1999) Mitochondria, Wiley-Liss, New York.
2. Saraste, M. (1999) Oxidative phosphorylation at the fin de siècle, Science 283, 1488-1493.
3. Walker, J. E. (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains, Q. Rev. Biophys. 25, 253-324.
4. Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., and Hirst, J. (2001) GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH: ubiquinone oxidoreductase (complex I), J. Biol. Chem. 276, 38345-38348.
5. Chomyn, A., Mariottini, P., Cleeter, M. W. J., Ragan, C. I., Matsuno-Yagi, A., Hatefi, Y., Doolittle, R. F., and Attardi, G. (1985) Six Unidentified Reading Frames of Human Mitochondrial DNA Encode Components of the Respiratory-Chain NADH Dehydrogenase, Nature 314, 591-597.
6. Chomyn, A., Cleeter, M. W. J., Ragan, C. I., Riley, M., Doolittle, R. F., and Attardi, G. (1986) URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit, Science 234, 614-618.
7. Feamley, I. M., and Walker, J. E. (1992) Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins, Biochim. Biophys. Acta 1140, 105-134.
8. Wallace, D. C. (1999) Mitochondrial diseases in man and mouse, Science 283, 1482-1488.
9. Jenner, P. (2001) Parkinson's disease, pesticides and mitochondrial dysfunction, Trends Neurosci. 24, 245-246.
10. Matsuno-Yagi, A., and Yagi, T., Eds. (2001) Complex I, J. Bioenerg. Biomembr. 33, 155-266.
11. Miyoshi, H. (1998) Structure-activity relationships of some complex 1 inhibitors, Biochim. Biophys. Acta 1364, 236-244.
12. Miyoshi, H. (2001) Probing the ubiquinone reduction site in bovine mitochondrial complex 1 using a series of synthetic ubiquinones and inhibitors, J. Bioenerg. Biomembr. 33, 223-231.
13. Earley, F. G., and Ragan, C. I. (1984) Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone, Biochem. J. 224, 525-534.
14. 3H]dihydrorotenone, FEBS Lett. 219, 108-113.
15. Yagi, T. (1987) Inhibition of NADH-ubiquinone reductase activity by N′,N′-dicyclohexylcabodiimide and correlation of this inhibition with the occurrence of energy coupling site 1 in various organisms, Biochemistry 26, 2822-2828.
16. Yagi, T., and Hatefi, Y. (1988) Identification of the DCCD-Binding Subunit of NADH-Ubiquinone Oxidoreductase (Complex I), J. Biol. Chem. 263, 16150-16155.
17. Hassinen, I. E., and Vuokila. P. T. (1993) Reaction of dicyclohexylcarbodiimide with mitochondrial proteins, Biochim. Biophys. Acta 1144, 107-124.
18. Heinrich, H., and Werner, S. (1992) Identification of the ubiquinone-binding site of NADH:ubiquinone oxidoreductase (complex I) from Neurospora crassa, Biochemistry 31, 11413-11419.
19. Heinrich, H., Azevedo, J. E., and Werner, S. (1992) Characterization of the 9.5-kDa ubiquinone-binding protein of NADH: ubiquinone oxidoreductase (complex 1) from Neurospora crassa, Biochemistry 31, 11420-11424.
20. Schuler, F., Yano, T., Di Bernardo, S., Yagi, T., Yankovskaya, V., Singer, T. P., and Casida, J. E. (1999) NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron - sulfur cluster N2 to quinone, Proc. Natl. Acad. Sci. U.S.A. 96, 4149-4153.
21. Ohnishi, T. (1998) Iron - sulfur clusters semiquinones in Complex I, Biochim. Biophys. Acta 1364, 186-206.
22. Darrouzet, E., Issartel, J. P., Lunardi, J., and Dupuis, A. 1998) The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors, FEBS Lett. 431, 34-38.
23. Dupuis, A., Prieur, I., and Lunardi, J. (2001) Toward a characterization of the connecting module of complex I, J. Bioenerg. Biomembr. 33, 159-168.
24. Kashani-Poor, N., Zwicker, K., Kerscher, S., and Brandt, U. (2001) A central functional role for the 49 kDa subunit within the catalytic core of mitochondrial complex I, J. Biol. Chem. 276, 24082-24087.
25. +-translocating NADH-quinone oxidoreductase, FEBS Lett. 508, 385-26.
26. Yagi, T., Di Bernardo, S., Nakamaru-Ogiso, E., Kao, M.-C., Seo, B. B., and Matsuno-Yagi, A. (2003) in Respiration in Archaea and Bacteria (Zannoni, D., Ed.) Kluwer Publishings, Dordrecht (in press).
27. Schuler, F., and Casida, J. E. (2001) Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling, Biochim. Biophys. Acta 1506, 79-87.
28. Matsuno-Yagi, A., and Hatefi, Y. (1985) Studies on the Mechanism of Oxidative Phosphorylation: Catalytic Site Cooperativity in ATP Synthesis, J. Biol. Chem. 260, 14424-14427.
29. Resek, J. F., Bhattacharya, S. K., and Khorana, H. G. (1993) A new photo-crosslinking reagent for the study of protein-protein interactions, J. Org. Chem. 58, 7598-7601.
30. +/2(e) stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles, FEBS Lett. 451, 157-161.
31. Laemmli, U. K. (1970) Nature 227, 680-685.
32. Schagger, H., and Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa, Anal. Biochem. 166, 368-379.
33. Schagger, H. (1995) Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes, Methods Enzymol. 260, 190-202.
34. Zerbetto, E., Vergani, L., and Dabbeni-Sala, F. (1997) Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels, Electrophoresis 18, 2059-2064.
35. O'Farrell, P. H. (1975) High-resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250, 4007-4021.
36. Herbert, B. (1999) Advances in protein solubilisation for two-dimensional electrophoresis. Electrophoresis 20, 660-663.
37. o Subunits, J. Biol. Chem. 266, 13564-13571.
38. Sazanov, L. A., Peak-Chew, S. Y., Fearnley, I. M., and Walker, J. E. (2000) Resolution of the membrane domain of bovine complex 1 into subcomplexes: implications for the structural organization of the enzyme, Biochemistry 39, 7229-7235.
39. Seo, B. B., Matsuno-Yagi, A., and Yagi, T. (1999) Modulation of oxidative phosphorylation of human kidney 293 cells by transfection with the internal rotenone-insensitive NADH-quinone oxidoreductase (NDII) gene of Saccharomyces cerevisiae, Biochim. Biophys. Acta 1412, 56-65.
40. Anderson, D. J., and Blobel, G. (1983) Immunoprecipitation of proteins from cell-free translation, Methods Enzymol. 96, 111-120.
41. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275.
42. 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.
43. 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.
44. Yamaguchi, M., Belogrudov, G. I., Matsuno-Yagi, A., and Hatefi, Y. (2000) The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I), Eur. J. Biochem. 267, 329-336.
45. Degli Esposti, M. (1998) Inhibitors of NADH-ubiquinone reductase: an overview, Biochim. Biophys. Acta 1364, 222-235.
46. Takano, S., Yano, T., and Yagi, T. (1996) Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH-I) of Paracoccus denitrificans: Identity, property, and stoichiometry of the peripheral subunits, Biochemistry 35, 9120-9127.
47. +-translocating NADH-quinoneoxidoreductase (NDH-1) of Paracoccus denitrificans: Studies on topology and stoichiometry of the peripheral subunits, J. Biol. Chem. 274, 28606-28611.
48. Ames, G. F., and Nikaido, K. (1976) Two-dimensional gel electrophoresis of membrane proteins, Biochemistry 15, 616-623.
49. Molloy, M. P. (2000) Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients, Anal. Biochem. 280, 1-10.
50. 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.
51. Dupuis, A., Skehel, J. M., and Walker, J. E. (1991) A homologue of a nuclear-coded iron - sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes, Biochemistry 30, 2954-2960.
52. Skehel, J. M., Fearnley, I. M., and Walker, J. E. (1998) NADH: Ubiquinone oxidoreductase from bovine heart mitochondria: sequence of a novel 17.2-kDa subunit, FEBS Lett. 438, 301-305.
53. + antiporter from Staphylococcus aureus, J. Bacteriol. 180, 6642-6648.
54. Friedrich, T., and Weiss, H. (1997) Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules, J. Theor. Biol. 187, 529-540.
55. + translocation by bacterial NADH:quinone oxidoreductases: an extension to the complex-I family of primary redox pumps, Biochim. Biophys. Acta 1505, 45-56.
56. + translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli, Mol. Microbiol. 35, 428-434.
57. Young-Mog, K., Tachibana, Y., Shimamoto, T., Shimamoto, T., and Tsuchiya, T. (1997) Inhibition of melibiose transporter by amiloride in Escherichia coli, Biochem. Biophys. Res. Commun. 233, 147-149.
58. + exchanger, NHEI: structure, regulation, and cellular actions, Annu. Rev. Pharmacol. Toxicol. 42, 527-552.
59. Sazanov, L. A., and Walker, J. E. (2000) Cryo-electron Crystallography of Two Sub-complexes of Bovine Complex I Reveals the Relationship between the Membrane and Peripheral Arms, J. Mol. Biol. 302, 455-464.
60. 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.
61. Belogrudov, G. I., and Hatefi, Y. (1994) Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): Subunit stoichiometry and substrate-induced conformation changes, Biochemistry 33, 4571-4576.
62. Vinogradov, A. D., and Grivennikova, V. G. (2001) The mitochondrial Complex I: progress in understanding of catalytic properties, IUBMB Life 52, 129-134.
63. Bottcher, B., Scheide, D., Hesterberg, M., Nagel-Steger, L., and Friedrich, T. (2002) A Novel, Enzymatically active conformation of the Escherichia coli NADH:Ubiquinone oxidoreductase (complex I), J. Biol. Chem. 277, 17970-17977.
64. +-translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: Implications for the mechanism of redox-driven cation translocation by complex I, J. Bioenerg. Biomembr. 33, 179-186.
65. Gemperli, A. C., Dimroth, P., and Steuber, J. (2002) The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump, J. Biol. Chem., 277, 33811-33817.
66. + antiporter from Vibrio parahaemolyticus, J. Bacteriol. 179, 7600-7602.
67. Bai, Y., Shakeley, R. M., and Attardi, G. (2000) Tight control of respiration by NADH dehydrogenase ND5 subunit gene expression in mouse mitochondria, Mol. Cell. Biol. 20, 805-815.
68. Hofhaus, G., and Attardi, G. (1995) Efficient selection and characterization of mutants of a human cell line which are defective in mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase, Mol. Cell. Biol. 15, 964-974.
69. Cardol, P., Matagne, R. F., and Remacle, C. (2002) Impact of Mutations Affecting ND Mitochondria-encoded Subunits on the Activity and Assembly of Complex I in Chlamydomonas. Implication for the Structural Organization of the Enzyme, J. Mol. Biol. 319, 1211-1221.
70. Roth, R., and Hagerhall, C. (2001) Transmembrane orientation and topology of the NADH:quinone oxidoreductase putative quinone binding subunit NuoH, Biochim. Biophys. Acta 1504, 352-362.
71. Di Bernardo, S., Yano, T., and Yagi, T. (2000) Exploring the Membrane Domain of the Reduced Nicotinamide Adenine Dinucleotide-Quinone Oxidoreductase of Paracoccus denitrificans: Characterization of the NQO7 Subunit, Biochemistry 39, 9411-9418.
72. Kao, M.-C., Di Bernardo, S., Matsuno-Yagi, A., and Yagi, T. (2002) Characterization of the Membrane Domain Nqol 1 Subunit of the Proton-Translocating NADH-Quinone Oxidoreductase of Paracoccus denitrificans, Biochemistry 41, 4377-4384.
73. Zickermann, V., Barquera, B., Wikström, M., and Finel, M. (1998) Analysis of the pathogenic human mitochondrial mutation ND 1/3460, and mutations of strictly conserved residues in its vicinity, using the bacterium Paracoccus denitrificans, Biochemistry 37, 11792-11796.
74. Kurki, S., Zickermann, V., Kervinen, M., Hassinen, I., and Finel, M. (2000) Mutagenesis of Three Conserved Glu Residues in a Bacterial Homologue of the ND1 Subunit of Complex I Affects Ubiquinone Reduction Kinetics but Not Inhibition by Dicyclohexylcarbodiimide, Biochemistry 39, 13496-13502.
75. Fisher, N., and Rich, P. R. (2000) A motif for quinone binding sites in respiratory and photosynthetic systems, J. Mol. Biol. 296, 1153-1162.