Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I

FEBS Letters

Volumn 579, Issue 2, 2005, Pages 500-506

  Ohnishi, Tomoko ^a   Johnson Jr , Jerry E ^b   Yano, Takahiro ^a   Lobrutto, Russell ^c   Widger, William R ^b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b University of Houston   (United States)

^c ARIZONA STATE UNIVERSITY   (United States)

Author keywords

E m; EPR spectrum; NADH:ubiquinone oxidoreductase; Ubisemiquinone

Indexed keywords

ANION; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

ARTICLE; CLUSTER ANALYSIS; COW; ELECTRIC POTENTIAL; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ISOLATED HEART; OXIDATION REDUCTION REACTION; PH; POTENTIOMETRY; PRIORITY JOURNAL; SAMPLE; SIGNAL DETECTION; TEMPERATURE; THERMODYNAMICS; TITRIMETRY;

ANIMALS; CATTLE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX I; MITOCHONDRIA, HEART; MYOCARDIUM; OXIDATION-REDUCTION; THERMODYNAMICS; UBIQUINONE;

BOVINAE;

EID: 11844287666     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.11.107     Document Type: Article

References (58)

1. Y. Hatefi The mitochondrial electron transport and oxidative phosphorylation system Ann. Rev. Biochem. 54 1985 1015 1069
2. H. Weiss, T. Friedrich, G. Hofhaus, and D. Preis The respiratory-chain NADH dehydrogenase (complex I) of mitochondria Eur. J. Biochem. 197 1991 563 576
3. T. Ohnishi Iron-sulfur clusters/semiquinones in complex I Biochim. Biophys. Acta 1364 1998 186 206
4. M. Saraste Oxidative phosphorylation at the fin de Siele Science 283 1999 1488 1493
5. J.E. Walker The NADH: ubiquinone oxidoreductase (complex I) of respiratory chains Q. Rev. Biophys. 25 1992 253 324
6. T. Yano The energy-transducing NADH: quinone oxidoreductase, complex I Mol. Aspects Med. 23 2002 345 368
7. G.C. Brown, and M.D. Brand Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio Biochem. J. 252 1988 473 479
8. F. Di Virgilio, and G.F. Azzone Activation of site I redox-driven H+ pump by exogenous quinones in intact mitochondria J. Biol. Chem. 257 1982 4106 4113
9. T.A. Scholes, and P.C. Hinkle Energetics of ATP-driven reverse electron transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles Biochemistry 23 1984 3341 3345
10. H. Weiss, and T. Friedrich Redox-linked proton translocation by NADH-ubiquinone reductase (complex I) J. Bioenerg. Biomembr. 23 1991 743 754
11. M. Wikström Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone FEBS Lett. 169 1984 300 304
12. +/2e stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles FEBS Lett. 451 1999 157 161
13. T. Yano, S. Magnitsky, V.D. Sled', T. Ohnishi, and T. Yagi Characterization of the putative 2x[4Fe-4S] binding NQO9 subunit of the proton translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: expression, reconstitution, and EPR characterization J. Biol. Chem. 274 1999 28598 28605
14. T. Rasmussen, D. Scheide, B. Brors, L. Kintscher, H. Weiss, and T. Friedrich Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I) Biochemistry 40 2001 6124 6131
15. + antiporter system of alkalophilic Bacillusspecies strain C-125 Molecular Microbiology 14 1994 939 946
16. M. Hiramatsu, K. Oikawa, H. Noda, A. Mori, T. Ogata, and H. Kamada Free radical imaging by electron spin resonance computed tomography in rat brain Brain Res. 697 1995 44 47
17. + antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters FEBS Lett. 496 2001 117 120
18. E. Nakamaru-Ogiso, K. Sakamoto, A. Matsuno-Yagi, H. Miyoshi, and T. Yagi The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I Biochemistry 42 2003 746 754
19. B. Amarneh, and S.B. Vik Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone Biochemistry 42 2003 4800 4808
20. X. Gong, T. Xie, L. Yu, M. Hesterberg, D. Scheide, T. Friedrich, and C.A. Yu The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli J. Biol. Chem. 278 2003 25731 25737
21. N. Fisher, and P.R. Rich A motif for quinone binding sites in respiratory and photosynthetic systems J. Mol. Biol. 296 2000 1153 1162
22. W.J. Ingledew, and T. Ohnishi An analysis of some thermodynamic properties of iron-sulfur centres in site I of mitochondria Biochem. J. 186 1980 111 117
23. T. Ohnishi Mitochondrial iron-sulfur flavodehydrogenases R.A. Capaldi Membrane Proteins in Energy Transduction 1979 Marcel Dekker, Inc New York 1 87
24. U. Brandt Proton-translocation by membrane-bound NADH:ubiquinone- oxidoreductase (complex I) through redox-gated ligand conduction Biochim. Biophys. Acta 1318 1997 79 91
25. P.L. Dutton, C.C. Moser, V.D. Sled, F. Daldal, and T. Ohnishi A reductant-induced oxidation mechanism for Complex I Biochim. Biophys. Acta 1364 1998 245 257
26. U. Brandt Proton translocation in the respiratory chain involving ubiquinone - A hypothetical semiquinone switch mechanism for complex I BioFactors 9 1999 95 101
27. P. Mitchell The protonmotive Q cycle: a general formulation FEBS Lett. 59 1975 137 139
28. A. Crofts, S. Meinhardt, K. Jones, and M. Snozzi The role of the quinone pool in the cyclic electron transfer chain of Q-cycle mechanism Biochim. Biophys. Acta 723 1983 202 218
29. J.R. Bowyer, and T. Ohnishi EPR spectroscopy in the study of ubisemiquinones in redox chains G. Lenaz Coenzyme Q 1985 John Wiley and Sons New York 409 432
30. B.L. Trumpower, and R.B. Gennis Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation Ann. Rev. Biochem. 63 1994 675 716
31. M.Y. Okamura, M.L. Paddock, M.S. Graige, and G. Feher Proton and electron transfer in bacterial reaction centers Biochim. Biophys. Acta 1458 2000 148 163
32. A.D. Vinogradov, V.D. Sled, D.S. Burbaev, V.G. Grivennikova, I.A. Moroz, and T. Ohnishi Energy-dependent complex I-associated ubisemiquinones in submitochondrial particles FEBS Lett. 370 1995 83 87
33. T. Ohnishi, S. Magnitsky, T. Toulokhonova, T. Yano, T. Yagi, D.S. Burbaev, A. Vinogradov, and V.D. Sled' EPR studies of the possible binding sites of the cluster N2, semiquinone, and specific inhibitors of the NADH:quinone oxidoreductase (complex I) Biochem. Soc. Trans. 27 1999 586 591
34. S. Magnitsky, L. Toulokhonova, T. Yano, V.D. Sled, C. Hägerhäll, V.G. Grivennikova, D.S. Burbaev, A.D. Vinogradov, and T. Ohnishi EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ J. Bioenerg. Biomembr. 34 2002 193 208
35. T. Yano, S. Magnitsky, and T. Ohnishi Characterization of the complex I-associated ubisemiquinone species: toward the understanding of their functional roles in the electron/proton transfer reaction Biochim. Biophys. Acta 1459 2000 299 304
36. J.C. Salerno, and T. Ohnishi Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system Biochem. J. 192 1980 769 781
37. T. Ohnishi, and B.L. Trumpower Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate-cytochrome c reductase complex J. Biol. Chem. 255 1980 3278 3284
38. A.B. Kotlyar, S.P.J. Albracht, and R.J. van Spanning Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria Biochim. Biophys. Acta 1365 1998 53 59
39. V.G. Grivennikova, R. Roth, N.V. Zakharova, C. Hägerhäll, and A.D. Vinogradov The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites Biochim. Biophys. Acta 1607 2003 79 90
40. Y. Hatefi Preparation and properties of NADH: ubiquinone oxidoreductase (complex I), EC 1.6.5.3 Methods Enzymol. 53 1978 11 14
41. C.I. Ragan, M.T. Wilson, V.M. Darley-Usmar, and P.N. Lowe Sub-fractionation of mitochondria and isolation of proteins of oxidative phosphorylation Mitochondria a Particle Approach vol. 4 1987 IRL Press Oxford 79 112
42. J.E. Johnson, K. Choksi, and W.R. Widger NADH-Ubiquinone oxidoreductase: substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide Mitochondrion 3 2003 97 110
43. P.L. Dutton Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems Methods Enzymol. 54 1978 411 435
44. R. Cammack, M.J. Barber, and R.C. Bray Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase Biochem. J. 157 1976 469 478
45. V.D. Sled, N.I. Rudnitzky, Y. Hatefi, and T. Ohnishi Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) Biochemistry 33 1994 10069 10075
46. Widger, W.R. (1979) Properties and activities associated with the NADH-ubiquinone reductase of the inner mitochondrial membrane from bovine cardiac muscles. Ph.D. thesis, State University of New York, Albany
47. T.E. King L. Yu S. Nagaoka W.R. Widger C.A. Yu Frontiers in Biological Energetics 1978 Academic Press New York, NY
48. W.J. Ingledew, T. Ohnishi, and J.C. Salerno Studies on a stabilization of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo Eur. J. Biochem. 227 1995 903 908
49. H. Ding, D.E. Robertson, F. Daldal, and P.L. Dutton Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model Biochemistry 31 1992 3144 3158
50. o-site of the bc1 complex controls the rate of ubihydroquinone oxidation Biochim. Biophys. Acta 1655 2004 77 92
51. T. Friedrich Complex I: a chimaera of a redox and conformation-driven proton pump? J. Bioenerg. Biomembr. 33 2001 169 177
52. B. Böttcher, D. Scheide, M. Hesterberg, L. Nagel-Steger, and T. Friedrich A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) J. Biol. Chem. 277 2002 17970 17977
53. T. Friedrich, and B. Böttcher The gross structure of the respiratory complex I: a Lego System Biochim. Biophys. Acta 1608 2004 1 9
54. L.A. Sazanov, S.Y. Peak-Chew, I.M. Fearnley, and J.E. Walker Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme Biochemistry 39 2000 7229 7235
55. A.A. Mamedova, P.J. Holt, J. Carroll, and L.A. Sazanov Substrate-induced conformational change in bacterial complex I J. Biol. Chem. 279 2004 23830 23836
56. G. Belogrudov, and Y. Hatefi Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): Subunit stoichiometry and substrate-induced conformation changes Biochemistry 33 1994 4571 4576
57. Y. Nakashima, K. Shinzawa-Itoh, K. Watanabe, K. Naoki, N. Hano, and S. Yoshikawa Steady-state kinetics of NADH:coenzyme Q oxidoreductase isolated from bovine heart mitochondria J. Bioenerg. Biomembr. 34 2002 11 19
58. S.W. Meinhardt, X. Yang, B.L. Trumpower, and T. Ohnishi Identification of a stable ubisemiquinone and characterization of the effects of ubiquinone oxidation-reduction status on the Rieske iron-sulfur protein in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans J. Biol. Chem. 262 1987 8702 8706