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Cluster N1 of complex I from Yarrowia lipolytica studied by pulsed EPR spectroscopy

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Abstract

After reduction with nicotinamide adenine dinucleotide (NADH), NADH:ubiquinone oxidoreductase (complex I) of the strictly aerobic yeast Yarrowia lipolytica shows clear signals from five different paramagnetic iron–sulfur (FeS) clusters (N1–N5) which can be detected using electron paramagnetic resonance (EPR) spectroscopy. The ligand environment and the assignment of several FeS clusters to specific binding motifs found in several subunits of the complex are still under debate. In order to characterize the hyperfine interaction of the surrounding nuclei with FeS cluster N1, one- and two-dimensional electron spin echo envelope modulation experiments were performed at a temperature of 30 K. At this temperature only cluster N1 contributes to the overall signal in a pulsed EPR experiment. The hyperfine and quadrupole tensors of a nitrogen nucleus and the isotropic and dipolar hyperfine couplings of two sets of protons could be determined by numerical simulation of the one- and two-dimensional spectra. The values obtained are in perfect agreement with a ferredoxin-like binding structure by four cysteine amino acid residues and allow the assignment of the nitrogen couplings to a backbone nitrogen nucleus and the proton couplings to the β-protons of the bound cysteine residues.

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Notes

  1. Although some resonances are difficult to detect [g zz (N3)] the EPR spectrum at 5 K shows the same features as the cw-EPR spectra previously recorded and cluster N3 can be clearly identified by its g xx component (indicated by the asterisk in Fig. 1).

References

  1. Videira A (1998) Biochim Biophys Acta 1364:89–100

    Article  PubMed  CAS  Google Scholar 

  2. Brandt U, Kerscher S, Dröse S, Zwicker K, Zickermann V (2003) FEBS Lett 545:9–17

    Article  PubMed  CAS  Google Scholar 

  3. Wikström MKF (1984) FEBS Lett 169:300–304

    Article  PubMed  Google Scholar 

  4. Weiss H, Friedrich T (1991) Biochim Biophys Acta 23:743–771

    CAS  Google Scholar 

  5. Shapira AH (1998) Biochim Biophys Acta 1364:261–270

    Article  PubMed  Google Scholar 

  6. Hirst J, Carroll J, Fearnley IM, Shannon J, Walker JE (2003) Biochim Biophys Acta 1604:135–150

    Article  PubMed  CAS  Google Scholar 

  7. Yagi T, Yano S, Di Bernado S, Matsuno-Yagi A (1998) Biochim Biophys Acta 1354:125–133

    Google Scholar 

  8. Yano T, Ohnishi T (2001) J Bioenerg Biomemb 33:213–222

    Article  CAS  Google Scholar 

  9. van Belzen R, Kotlyar AB, Moon N, Dunham WR, Albracht SPJ (1997) Biochemistry 36:886–893

    Article  PubMed  Google Scholar 

  10. Ohnishi T (1998) Biochim Biophys Acta 1364:186–206

    Article  PubMed  CAS  Google Scholar 

  11. Rasmussen T, Scheide D, Brors B, Kintscher L, Weiss H, Friedrich T (2001) Biochemistry 40:6124–6131

    Article  PubMed  CAS  Google Scholar 

  12. Nakamaru-Ogiso E, Yano T, Yagi T, Ohnishi O (2005) J Biol Chem 280:301–307

    PubMed  CAS  Google Scholar 

  13. Hinchliffe P, Sazanov LA (2005) Science 309:771–774

    Article  PubMed  CAS  Google Scholar 

  14. Yano T (2003) J Biol Chem 278:15514–15522

    Article  PubMed  CAS  Google Scholar 

  15. Waletko A, Zwicker K, Abdrakhmanova A, Zickermann V, Brandt U, Kerscher S (2005) J Biol Chem 280:5622–5625

    Article  PubMed  CAS  Google Scholar 

  16. Maly T, MacMillan F, Zwicker K, Kashani-Poor N, Brandt U, Prisner T (2004) Biochemistry 43:3969–3978

    Article  PubMed  CAS  Google Scholar 

  17. Maly T, Prisner T (2004) J Magn Reson 170:88–96

    Article  PubMed  CAS  Google Scholar 

  18. Deligiannakis Y, Louloudi M, Hadjiliadis N (2000) Coord Chem Rev 204:1–112

    Article  CAS  Google Scholar 

  19. Kerscher S, Dröse S, Zwicker K, Zickermann V, Brandt U (2002) Biochim Biophys Acta 1555:83–91

    Article  PubMed  CAS  Google Scholar 

  20. Dröse S, Zwicker K, Brandt U (2002) Biochim Biophys Acta 1556:65–72

    Article  PubMed  Google Scholar 

  21. Kashani-Poor N, Kerscher S, Zickermann V, Brandt U (2001) Biochim Biophys Acta 1504:363–370

    Article  PubMed  CAS  Google Scholar 

  22. Djafarzadeh R, Kerscher S, Zwicker K, Rademacher M, Lindahl M, Schägger H, Brandt U (2000) Biochim Biophys Acta 1459:230–238

    Article  PubMed  CAS  Google Scholar 

  23. Mims WB (1972) Phys Rev B 5:2409–2419

    Article  Google Scholar 

  24. Höfer P, Grupp A, Nebenführ H, Mehring M (1986) Chem Phys Lett 132:279–282

    Article  Google Scholar 

  25. Gemperle C, Aebli G, Schweiger A, Ernst RR (1990) J Magn Reson 88:241–256

    CAS  Google Scholar 

  26. Bowman MK, Massoth RJ (1987) In: Weil JA (ed) Electron magnetic resonance of the solid state. The Canadian Society for Chemistry, Ottawa, pp 99–110

  27. Wang D-C, Meinhardt SW, Sackmann H, Weiss H, Ohnishi T (1991) Eu J Biochem 197:257–264

    Article  CAS  Google Scholar 

  28. Mouesca J-M, Lamotte B (1998) Coord Chem Rev 178–180:1573–1614

    Article  Google Scholar 

  29. Noodelman L, Lovell T, Liu T, Himo F, Torres RA (2002) Curr Opin Chem Biol 6:259–273

    Article  PubMed  Google Scholar 

  30. Dikanov SA, Xun L, Karpiel AB, Tyryshkin AM, Bowman MK (1996) J Am Chem Soc 118:8408–8416

    Article  CAS  Google Scholar 

  31. Gurbiel RJ, Batie CJ, Sivaraja M, True AE, Fee JA, Hoffmann BM, Ballou DP (1989) Biochemistry 28:4861–4871

    Article  PubMed  CAS  Google Scholar 

  32. Gurbiel RJ, Ohnishi T, Robertson DE, Daldal F, Hoffmann BM (1991) Biochemistry 30:11579–11584

    Article  PubMed  CAS  Google Scholar 

  33. Britt RD, Sauer K, Klein MP, Knaff DB, Kriauciunas A, Yu CA, Yu L, Malkin R (1991) Biochemistry 30:1892–1901

    Article  PubMed  CAS  Google Scholar 

  34. Shergill JK, Cammack R (1994) Biochim Biophys Acta 1185:43–49

    Article  PubMed  CAS  Google Scholar 

  35. Dikanov SA, Bowman MK (1995) J Magn Reson A 116:125–128

    Article  CAS  Google Scholar 

  36. Dikanov SA, Tyryshkin AM, Bowman MK (2000) J Magn Reson 144:228–242

    Article  PubMed  CAS  Google Scholar 

  37. Dikanov SA, Bowman MK (1998) J Biol Inorg Chem 3:18–29

    Article  CAS  Google Scholar 

  38. Mouesca J-M, Rius G, Lamotte B (1993) J Am Chem Soc 115:4714–4731

    Article  CAS  Google Scholar 

  39. Canne C, Ebelshäuser M, Gay E, Shergill JK, Cammack R, Kappl R, Hütermann J (2000) J Biol Inorg Chem 5:514–526

    Article  PubMed  CAS  Google Scholar 

  40. Kappl R, Ciurli S, Luchinat C, Hütermann J (1999) J Am Chem Soc 121:1925–1935

    Article  CAS  Google Scholar 

  41. Riedel A, Fetzner S, Rampp M, Lingens F, Liebl U, Zimmermann J-L, Nitschke W (1995) J Biol Chem 270:30869–30873

    Article  PubMed  CAS  Google Scholar 

  42. Shergill JK, Joannou CL, Mason JR, Cammack R (1995) Biochemistry 34:16533–16542

    Article  PubMed  CAS  Google Scholar 

  43. Shergill JK, Golinelli M-P, Cammack R, Meyer J (1996) Biochemistry 35:12842–12848

    Article  PubMed  CAS  Google Scholar 

  44. Cammack R, Chapman A, McCracken J, Peisach J (1991) J Chem Soc Faraday Trans 87:3203–3206

    Article  CAS  Google Scholar 

  45. Dikanov SA, Tyryshkin AM, Felli I, Reijerse EJ, Hütermann J (1995) J Magn Reson 108:99–102

    Article  CAS  Google Scholar 

Download references

Acknowledgements

This work was supported by the Sonderforschungsbereich SFB 472 “Molecular Bio-energetics.” The authors also want to thank the two anonymous reviewers for their helpful comments and suggestions.

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  1. T. Maly

    Present address: Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA

Authors and Affiliations

  1. Institut für Physikalische und Theoretische Chemie and Center for Biological Magnetic Resonance, Johann-Wolfgang-Goethe-Universität Frankfurt, 60439, Frankfurt am Main, Germany

    T. Maly & T. Prisner

  2. Zentrum der Biologischen Chemie, Universitätsklinikum Frankfurt, Molekulare Bioenergetik, 60590, Frankfurt am Main, Germany

    L. Grgic, K. Zwicker, V. Zickermann & U. Brandt

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  1. T. Maly
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Correspondence to T. Prisner.

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Maly, T., Grgic, L., Zwicker, K. et al. Cluster N1 of complex I from Yarrowia lipolytica studied by pulsed EPR spectroscopy. J Biol Inorg Chem 11, 343–350 (2006). https://doi.org/10.1007/s00775-006-0081-1

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  • DOI: https://doi.org/10.1007/s00775-006-0081-1

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