Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1777, Issue 7-8, 2008, Pages 703-710

  Ohnishi, Tomoko ^a   Nakamaru Ogiso, Eiko ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Complex I; EPR; Iron sulfur cluster; NADH Q oxidoreductase; Site directed mutagenesis

Indexed keywords

IRON SULFUR PROTEIN; LIGAND; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (QUINONE);

ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; EXPERIMENT; MICROWAVE RADIATION; MUTAGENESIS; NONHUMAN; PREDICTION; PRIORITY JOURNAL; REVIEW; SAMPLE; TEMPERATURE;

BACTERIAL PROTEINS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX I; ESCHERICHIA COLI PROTEINS; INDICATORS AND REAGENTS; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; QUINONE REDUCTASES; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); BOVINAE;

EID: 50949130428     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.04.032     Document Type: Review

References (42)

1. Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25 (1992) 253-324
2. Ohnishi T. Iron-sulfur clusters/semiquinones in Complex I. Biochim. Biophys. Acta 1364 (1998) 186-206
3. Yagi T., and Matsuno-Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry 42 (2003) 2266-2274
4. Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thernus thermophilus. Science 311 (2006) 1430-1436
5. Sazanov L.A. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 46 (2007) 2275-2288
6. Yano T., Sklar J., Nakamaru-Ogiso E., Takahashi Y., Yagi T., and Ohnishi T. Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans. J. Biol. Chem. 278 (2003) 15514-15522
7. Nakamaru-Ogiso E., Yano T., Ohnishi T., and Yagi T. Characterization of the iron-sulfur cluster coordinated by a cysteine cluster motif (CXXCXXXCX27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8. J. Biol. Chem. 277 (2002) 1680-1688
8. Nakamaru-Ogiso E., Yano T., Yagi 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
9. Nf) and the interaction with cluster N2: new insight into the energy-coupled electron transfer in complex I. Biochemistry 44 (2005) 1744-1754
10. Ohnishi T., and Salerno J.C. Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase. FEBS Lett. 579 (2005) 45-55
11. Yakovlev G., Reda T., and Hirst J. Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 12720-12725
12. E. Nakamaru-Ogiso, A. Matsuno-Yagi, S. Yoshikawa, T. Yagi and T. Ohnishi, Iron-sulfur cluster N5 is coordinated by a HxxxCxxCxxxxxC motif in the NuoG subunit of E. coli Complex I . (submitted for publication).
13. Leif H., Sled V.D., Ohnishi T., Weiss H., and Friedrich T. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230 (1995) 538-548
14. Djafarzadeh R., Kerscher S., Zwicker K., Radermacher M., Lindahl M., Schagger 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
15. Waletko A., Zwicker K., Abdrakhmanova A., Zickerman 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
16. Belevich G., Euro L., Wikström M., and Verkhovskaya M. Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli. Biochemistry 46 (2007) 526-533
17. Ohnishi T. Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart. Biochim. Biophys. Acta 387 (1975) 475-490
18. Wang D.-C., Meinhardt S.W., Sackmann U., Weiss H., and Ohnishi T. The iron-sulfur clusters in the two related forms of mitochondrial NADH:ubiquinone oxidoreductase made by Neurospora crassa. Eur. J. Biochem. 197 (1991) 257-264
19. Ohnishi T., Blum H., Galante Y.M., and Hatefi Y. Iron-sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase. J. Biol. Chem. 256 (1981) 9216-9220
20. Blumberg W.E., and Peisach J. On the interpretation of electron paramagnetic resonance spectra of binuclear iron-sulfur proteins. Arch. Biochem. Biophys. 162 (1974) 502-512
21. Uhlmann M., and Friedrich T. EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a. Biochemistry 44 (2005) 1653-1658
22. Ragan C.I., Galante Y.M., Hatefi Y., and Ohnishi T. Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins. Biochemistry 21 (1982) 590-594
23. Yano T., Sled V.D., Ohnishi T., and Yagi T. Expression of the 25 Kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans. Biochemistry 33 (1994) 494-499
24. 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
25. Yano T., Yagi T., Sled' V.D., and Ohnishi T. Expression and characterization of the 66-Kilodalton (Nqo3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 270 (1995) 18264-18270
26. Meinhardt S.W., Kula T., Yagi T., Lillich T., and Ohnishi T. EPR characterization of the iron-sulfur clusters in the NADH:ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans. J. Biol. Chem. 262 (1987) 9147-9153
27. Pohl T., Uhlmann M., Kaufenstein M., and Friedrich T. Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochemistry 46 (2007) 10694-10702
28. 1+ cluster with spin S = 3/2. J. Biol. Chem. 260 (1985) 11160-11173
29. Peters J.W., Lanzilotta W.N., Lemon B.J., and Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282 (1998) 1853-1858
30. Yano T., Magnitsky S., Sled' V.D., Ohnishi T., and Yagi T. 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
31. 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
32. Dupuis A., Chevallet M., Darrouzet E., Duborjal H., Lunardi J., and Issartel J.P. The Complex I from Rhodobacter capsulatus. Biochim. Biophys. Acta 1364 (1998) 147-165
33. Mathews R., Charlton S., Sands R.H., and Palmer G. On the nature of the spin coupling between the iron-sulfur clusters in the eight-iron ferredoxins. J. Biol. Chem. 249 (1974) 4326-4328
34. Prince R.C., and Adams M.W. Oxidation-reduction properties of the two Fe4S4 clusters in Clostridium pasteurianum ferredoxin. J. Biol. Chem. 262 (1987) 5125-5128
35. Maly T., McMillan F., Zwicker K., Kashani-Poor N., Brandt U., and Prisner T.F. Relaxation filtered hyperfine (REFINE) spectroscopy: a novel tool for studying overlapping biological electron paramagnetic resonance signals applied to mitochondrial complex I. Biochemistry 43 (2004) 3969-3978
36. Prisner T.F., Rohrer M., and MacMillan F. Pulsed EPR spectroscopy: biological applications. Ann. Rev. Phys. chem. 52 (2001) 279-313
37. Hellwig P., Scheide D., Bungert S., Mantele W., and Friedrich T. 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 (2000) 10884-10891
38. Sugiyama H., Nakatsubo R., Yamaguchi S., Ogura T., Shinzawa-Itoh K., and Yoshikawa S. Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system. J. Bioenerg. Biomembr. 39 (2007) 145-148
39. Hinchliffe P., Carroll J., and Sazanov L.A. Identification of a novel subunit of respiratory complex I from Thermus thermophilus. Biochemistry 45 (2006) 4413-4420
40. Fernandes A.S., Sousa F.L., Teixeira M., and Pereira M.M. Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus. Biochemistry 45 (2006) 1002-1008
41. Meinhardt S.W., Wang D.-C., Hon-nami K., Yagi T., Oshima T., and Ohnishi T. Studies on the NADH-Q oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8. J. Biol. Chem. 265 (1990) 1360-1368
42. Sled' V.D., Friedrich T., Leif H., Weiss H., Meinhardt S.W., Fukumori Y., Calhoun M.W., Gennis R.B., and Ohnishi T. Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems. J. Bioenerg. Biomembr. 25 (1993) 347-356