Characterization of a subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (complex I) lacking the flavoprotein part of the N-module

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1767, Issue 5, 2007, Pages 393-400

  Zickermann, Volker ^a   Zwicker, Klaus ^a   Tocilescu, Maja A ^a   Kerscher, Stefan ^a   Brandt, Ulrich ^a  

^a GOETHE UNIVERSITY   (Germany)

Author keywords

Complex I; Iron sulfur cluster; N module; NADH binding; NADH:ubiquinone oxidoreductase; Subcomplex; Yarrowia lipolytica

Indexed keywords

FLAVOPROTEIN; IRON; MITOCHONDRIAL ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFUR;

ARTICLE; BINDING SITE; ELECTRON; ELECTRON TRANSPORT; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SUBUNIT; FUNGUS; MAMMAL; NONHUMAN; NUCLEOTIDE BINDING SITE; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; REDUCTION; SITE DIRECTED MUTAGENESIS; TITRIMETRY;

BACTERIAL PROTEINS; CATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX I; FLAVIN MONONUCLEOTIDE; FLAVOPROTEINS; MUTAGENESIS, SITE-DIRECTED; SEQUENCE DELETION; YERSINIA;

MAMMALIA; YARROWIA LIPOLYTICA;

EID: 34247530881     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.03.005     Document Type: Article

References (33)

1. Brandt U. Energy converting NADH:quinone oxidoreductases. Annu. Rev. Biochem. 75 (2006) 69-92
2. Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
3. Radermacher M., Ruiz T., Clason T., Benjamin S., Brandt U., and Zickermann V. The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme. J. Struct. Biol. 154 (2006) 269-279
4. Friedrich T., Steinmüller K., and Weiss H. The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367 (1995) 107-111
5. 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
6. 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
7. Carroll J., Fearnley I.M., Shannon R.J., Hirst J., and Walker J.E. Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell Proteomics 2 (2003) 117-126
8. Abdrakhmanova A., Zwicker K., Kerscher S., Zickermann V., and Brandt U. 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 (2006) 1676-1682
9. Yamaguchi M., Belogrudov G., Matsuno-Yagi A., and Hatefi Y. The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 267 (2000) 329-336
10. Galante Y.M., and Hatefi Y. Resolution of complex I and isolation of NADH dehydrogenase and an iron-sulfur protein. Methods Enzymol. 53 (1978) 15-21
11. 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
12. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
13. Rais I., Karas M., and Schägger H. Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics 4 (2004) 2567-2571
14. Waletko A., Zwicker K., Abdrakhmanova A., Zickermann V., Brandt U., and Kerscher S. Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity. J. Biol. Chem. 280 (2005) 5622-5625
15. Okun J.G., Zickermann V., Zwicker K., Schägger H., and Brandt U. Binding of detergents and inhibitors to bovine complex I-A novel purification procedure of bovine complex I retaining full inhibitor sensitivity. Biochim. Biophys. Acta 1459 (2000) 77-87
16. 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 1556 (2002) 65-72
17. 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
18. Garofano A., Zwicker K., Kerscher S., Okun P., and Brandt U. Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity. J. Biol. Chem. 278 (2003) 42435-42440
19. Galante Y.M., and Hatefi Y. Purification and molecular and enzymatic properties of mitochondrial NADH dehydrogenase. Arch. Biochem. Biophys. 192 (1979) 559-568
20. Finel M., Skehel J.M., Albracht S.P.J., Fearnley I.M., and Walker J.E. Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry 31 (1992) 11425-11434
21. Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., and Walker J.E. Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry 39 (2000) 7229-7235
22. Galkin A., Dröse S., and Brandt U. The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes. Biochim. Biophys. Acta 1757 (2006) 1575-1581
23. 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
24. 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
25. Pilkington S.J., Skehel J.M., Gennis R.B., and Walker J.E. Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 30 (1991) 2166-2175
26. Albracht S.P.J., and Hedderich R. Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (ComplexI). FEBS Lett. 24275 (2000) 1-6
27. Gavrikova E.V., Grivennikova V.G., Sled V.D., Ohnishi T., and Vinogradov A.D. Kinetics of the mitochondrial three-subunit NADH dehydrogenase interaction with hexammineruthenium(III). Biochim. Biophys. Acta 1230 (1995) 23-30
28. Fearnley I.M., and Walker J.E. Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta 1140 (1992) 105-134
29. Fecke W., Sled V.D., Ohnishi T., and Weiss H. Disruption of the gene encoding the NADH-binding subunit of NADH: ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3. Eur. J. Biochem. 220 (1994) 551-558
30. Yano T., Sled V.D., Ohnishi T., and Yagi T. Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 5-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Pracoccus denitrificans. J. Biol. Chem. 271 (1996) 5907-5913
31. Ohnishi T. Iron-sulfur clusters semiquinones in complex I. Biochim. Biophys. Acta 1364 (1998) 186-206
32. Nakamaru-Ogiso E., Yano T., and Ohnishi T. Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. J. Biol. Chem. 280 (2005) 301-307
33. Zu Y., Di Bernardo S., Yagi T., and Hirst J. Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (Complex I). Biochemistry 41 (2002) 10056-10069