The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 12, 2006, Pages 1575-1581

  Galkin, Alexander ^a   Dröse, Stefan ^a   Brandt, Ulrich ^a  

^a GOETHE UNIVERSITY   (Germany)

Author keywords

Complex I; Energy transduction; Mitochondria; NADH:ubiquinone oxidoreductase; Proteoliposome; Proton pump

Indexed keywords

PROTON PUMP; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

ARTICLE; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME PURIFICATION; ENZYME RECONSTITUTION; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEOLIPOSOME; STOICHIOMETRY; YARROWIA LIPOLYTICA; YEAST;

AEROBIOSIS; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX I; MEMBRANE POTENTIALS; MITOCHONDRIA; OXIDATIVE PHOSPHORYLATION; PROTEOLIPIDS; PROTON PUMPS; YARROWIA;

YARROWIA LIPOLYTICA;

EID: 33751556659     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.10.001     Document Type: Article

References (53)

1. Brandt U. Energy converting NADH:quinone oxidoreductases. Annu. Rev. Biochem. 75 (2006) 69-92
2. Wikström M.K.F. Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett. 169 (1984) 300-304
3. - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451 (1999) 157-161
4. Carroll J., Fearnley I.M., Skehel J.M., Shannon R.J., Hirst J., and Walker J.E. Bovine complex I is a complex of forty-five different subunits. J. Biol. Chem. 281 (2006) 32724-32727
5. Ohnishi T. Iron-sulfur clusters/ semiquinones in complex I. Biochim. Biophys. Acta 1364 (1998) 186-206
6. Rasmussen T., Scheide D., Brors B., Kintscher L., Weiss H., and Friedrich T. Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry 40 (2001) 6124-6131
7. Ohnishi T., Johnson J.E., Yano T., LoBrutto R., and Widger W.R. Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I. FEBS Lett. 579 (2005) 500-506
8. Nf) and the interaction with cluster N2: new insight into the energy-coupled electron transfer in complex I. Biochemistry 44 (2005) 1744-1754
9. Brandt U. Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction. Biochim. Biophys. Acta 1318 (1997) 79-91
10. Mitchell P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 41 (1966) 445-502
11. Krishnamoorthy G., and Hinkle P.C. Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase. J. Biol. Chem. 263 (1988) 17566-17575
12. De Vault D. Theory of iron-sulfur center N-2 oxidation and reduction by ATP. J. Theor. Biol. 62 (1976) 115-139
13. Kotlyar A.B., Sled V.D., Burbaev D.S., Moroz I.A., and Vinogradov A.D. Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles. FEBS Lett. 264 (1990) 17-20
14. Dutton P.L., Moser C.C., Sled V.D., Daldal F., and Ohnishi T. A reductant-induced oxidation mechanism for Complex I. Biochim. Biophys. Acta 1364 (1998) 245-257
15. Brandt U. Proton translocation in the respiratory chain involving ubiquinone - a hypothetical semiquinone switch mechanism for complex I. BioFactors 9 (1999) 95-101
16. Ohnishi T., and Salerno J.C. Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I). FEBS Lett. 579 (2005) 4555-4561
17. Zickermann V., Bostina M., Hunte C., Ruiz T., Radermacher M., and Brandt U. Functional implications from an unexpected position of the 49 kDa subunit of complex I. J. Biol. Chem. 278 (2003) 29072-29078
18. Kervinen M., Patsi J., Finel M., and Hassinen I.E. A pair of membrane-embedded acidic residues in the NuoK subunit of Escherichia coli NDH-1, a counterpart of the ND4L subunit of the mitochondrial complex I, are required for high ubiquinone reductase activity. Biochemistry 43 (2004) 773-781
19. Grgic L., Zwicker K., Kashani-Poor N., Kerscher S., and Brandt U. Functional significance of conserved histidines and arginines in the 49 kDa subunit of mitochondrial complex I. J. Biol. Chem. 279 (2004) 21193-21199
20. Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
21. Yamaguchi M., Belogrudov G., and Hatefi Y. Mitochondrial NADH-ubiquinone oxidoreductase (complex I). Effect of substrates on the fragmentation of subunits by trypsin. J. Biol. Chem. 273 (1998) 8094-8098
22. Böttcher B., Scheide D., Hesterberg M., Nagel-Steger L., and Friedrich T. A novel, enzymatically active conformation of the Escherichia coli NADH: ubiquinone oxidoreductase (Complex I). J. Biol. Chem. 277 (2002) 17970-17977
23. Brandt U., Kerscher S., Dröse S., Zwicker K., and Zickermann V. Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?. FEBS Lett. 545 (2003) 9-17
24. Mamedova A.A., Holt P.J., Carroll J., and Sazanov L.A. Substrate-induced conformational change in bacterial complex I. J. Biol. Chem. 279 (2004) 23830-23836
25. Zwicker K., Galkin A., Dröse S., Grgic L., Kerscher S., and Brandt U. The redox-Bohr group associated with iron-sulfur cluster N2 of complex I. J. Biol. Chem. 281 (2006) 23013-23017
26. Abdrakhmanova A., Zickermann V., Bostina M., Radermacher M., Schägger H., Kerscher S., and Brandt U. Subunit composition of mitochondrial complex I from the yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1658 (2004) 148-156
27. Abdrakhmanova A., Dobrynin K., Zwicker K., Kerscher S., and Brandt U. Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters. FEBS Lett. 579 (2005) 6781-6785
28. Djafarzadeh R., Kerscher S., Zwicker K., Radermacher M., Lindahl M., Schägger H., and Brandt U. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1459 (2000) 230-238
29. Kerscher S., Dröse S., Zwicker K., Zickermann V., and Brandt U. Yarrowia lipolytica, a yeast genetic system to study mitochondrial complex I. Biochim. Biophys. Acta, Bioenerg. 1555 (2002) 83-91
30. Dröse S., Zwicker K., and Brandt U. Full recovery of the NADH:ubiquinone activity of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids. Biochim. Biophys. Acta, Bioenerg. 1556 (2002) 65-72
31. Dröse S., Galkin A., and Brandt U. Proton pumping by complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica reconstituted into proteoliposomes. Biochim. Biophys. Acta, Bioenerg. 1710 (2005) 87-95
32. Zvyagilskaya R., Andreishcheva E., Soares M.I.M., Khozin I., Berhe A., and Persson B.L. Isolation and characterization of a novel leaf-inhabiting osmo-, salt-, and alkali-tolerant Yarrowia lipolytica yeast strain. J. Basic Microbiol. 41 (2001) 289-303
33. Azzone G.F., Colonna R., and Ziche B. Preparation of bovine heart mitochondria in high yield. Methods Enzymol. 55 (1979) 46-50
34. Estabrook R.W., and Maitra P.K. A fluorimetric method for the quantitative microanalysis of adenine and pyridine nucleotides. Anal. Biochem. 3 (1962) 369-382
35. Kerscher S., Okun J.G., and Brandt U. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell. Sci. 112 (1999) 2347-2354
36. Kashani-Poor N., Kerscher S., Zickermann V., and Brandt U. Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1504 (2001) 363-370
37. Cooper C.E., Bruce B.D., and Nicholls P. Use of oxonol V as a probe of membrane potential in proteoliposomes containing cytochrome oxidase in the submitochondrial orientation. Biochemistry 29 (1990) 3859-3865
38. Vinogradov A.D. Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta 1364 (1998) 169-185
39. Maklashina E., Kotlyar A.B., and Cecchini G. Active/de-active transition of respiratory complex I in bacteria, fungi, and animals. Biochim. Biophys. Acta 1606 (2003) 95-103
40. G.Medentsev A., and Akimenko V.K. Development and activation of cyanide-resistant respiration in the yeast Yarrowia lipolytica. Biochemistry 64 (1999) 945-951
41. Akimenko V.K., Trutko S.M., Medentsev A.G., and Korobov V.P. Distribution of cyanide-resistant respiration among yeasts and bacteria and its relation to oversynthesis of metabolites. Arch. Microbiol. 136 (1983) 234-241
42. Eschemann A., Galkin A., Oettmeier W., Brandt U., and Kerscher S. HDQ (1-Hydroxy-2-dodecyl-4(1H)quinolone), a high affinity inhibitor for mitochondrial alternative NADH dehydrogenase. J. Biol. Chem. 280 (2005) 3138-3142
43. +/Site ratio of mitochondrial electron transport with the oxygen pulse technique. J. Biol. Chem. 251 (1976) 5670-5679
44. Mitchell P., and Moyle J. Respiration-driven proton translocation in rat liver mitochondria. Biochem. J. 105 (1967) 1147-1162
45. Wikström M.K.F., Krab K., and Saraste M. Proton-translocating cytochrome complexes. Annu. Rev. Biochem. 50 (1981) 623-655
46. 1 complex. Biochim. Biophys. Acta 1275 (1996) 41-46
47. Heinz E., Westerhoff H.V., and van Dam K. The residual protonmotive force in mitochondria after an oxygen pulse. Eur. J. Biochem. 115 (1981) 107-113
48. Zharova T.V., and Vinogradov A.D. A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) by ADP-ribose. Biochim. Biophys. Acta 1320 (1997) 256-264
49. Bashford C.L., and Thayer W.S. Thermodynamics of the electrochemical proton gradient in bovine heart submitochondrial particles. J. Biol. Chem. 252 (1977) 8459-8463
50. Wikström M.K.F., and Penttilä T. Critical evaluation of the proton-translocating property of cytochrome oxidase in rat liver mitochondria. FEBS Lett. 144 (1982) 183-189
51. Verkhovskaya M., Verkhovsky M., and Wikström M. pH-Dependence of Proton Translocation by Escherichia coli. J. Biol. Chem. 267 (1992) 14559-14562
52. Ragan C.I., and Hinkle P.C. Ion transport and respiratory control in vesicles formed from reduced nicotinamid adenine dinucleotide coenzyme Q reductase and phospholipids. J. Biol. Chem. 250 (1975) 8472-8476
53. Hinkle P.C., Kumar A.M., Resetar A., and Harris D.A. Mechanistic stoichiometry of mitochondrial oxidative phosphorylation. Biochemistry 30 (1991) 3576-3582