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2006 | 109 | 3 | 237-247
Article title

Mössbauer Studies of Cu(II) Ions Interaction with the Non-Heme Iron and Cytochrome b_{559} in a Chlamydomonas reinhardtii PSI Minus Mutant

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EN
Mössbauer spectroscopy was applied, for the first time, to study the interaction of copper ions with the non-heme iron and the heme iron of cytochrome b_{559} in photosystem II thylakoids isolated from a Chlamydomonas reinhardtii photosystem I minus mutant. We showed that copper ions oxidize the heme iron and change its low spin state into a high spin state. This is probably due to deprotonation of the histidine coordinating the heme. We also found that copper preserves the non-heme iron in a low spin ferrous state, enhancing the covalence of iron bonds as compared to the untreated sample. We suggest that a disruption of hydrogen bonds stabilizing the quinone-iron complex by Cu^{2+} is the mechanism responsible for a new arrangement of the binding site of the non-heme iron leading to its more "tense" structure. Such a diamagnetic state of the non-heme iron induced by copper results in a magnetic decoupling of iron from the primary quinone acceptor. These results indicate that Cu does not cause removal of the non-heme iron from its binding site. The observed Cu^{2+} action on the non-heme iron and cytochrome b_{559} is similar to that previously observed forα-tocopherol quinone.
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author
  • Institute of Physics, Jagiellonian University, Reymonta 4, 30-059 Kraków, Poland
  • Institute of Nuclear Physics, Polish Academy of Sciences, Radzikowskiego 152, 31-342 Krakó Poland
author
  • Faculty of Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland
author
  • Faculty of Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland
author
  • Institute of Physics, Jagiellonian University, Reymonta 4, 30-059 Kraków, Poland
author
  • University of Bielefeld, Department of Biology, Molecular Cell Physiology, Universitaetsstr. 25, 33501 Bielefeld, Germany
author
  • University of Bielefeld, Department of Biology, Molecular Cell Physiology, Universitaetsstr. 25, 33501 Bielefeld, Germany
References
  • 1. W. Kaim, B. Schwederski, Bioorganic Chemistry: Inorganic Elements in the Chemistry of Life. An Introduction and Guide, Wiley, Chichester 1995
  • 2. K. Burda, J. Kruk, K. Strzalka, G.H. Schmid, Z. Naturforsch. C, 57, 853, 2002
  • 3. M. Droppa, G. Horváth, Plant. Sci., 9, 111, 1990
  • 4. M. Barón, J.B. Arellano, J.L. Gorge, Physiol. Plantarum, 94, 174, 1995
  • 5. B.-D. Hsu, J.-Y. Lee, Plant Physiol., 87, 116, 1988
  • 6. G. Vierke, P. Stuckmeier, Z. Naturforsch. C, 32, 605, 1977
  • 7. H.M. Haberman, Plant Physiol., 44, 331, 1969
  • 8. J.A. Cedeno-Maldomado, J.A. Swader, Plant Physiol., 50, 698, 1972
  • 9. G. Samuelson, G. Öquist, Plant Cell Physiol., 21, 445, 1980
  • 10. F. Sersen, K. Kralová, A. Bumbalová, O. Svajlenová, J. Plant Physiol., 151, 299, 1997
  • 11. W.P. Schröder, J.B. Arellano, T. Bittner, M. Barón, H.J. Eckert, G. Renger, J. Biol. Chem., 269, 32865, 1994
  • 12. C. Jegerschöld, J.B. Arellano, W.P. Schröder, P.J. van Kan, M. Barón, S. Styring, Biochemistry, 34, 12747, 1995
  • 13. J. Yruela, G. Gatzen, R. Picorel, A.R. Holtzwarth, Biochemistry, 35, 9469, 1996
  • 14. D.P. Singh, S.P. Singh, Plant Physiol., 83, 12, 1987
  • 15. C. Jegerschöld, F. MacMillan, W. Lubitz, A.W. Rutherford, Biochemistry, 38, 12439, 1999
  • 16. J.N. Mohanty, I. Vass, S. Demeter, Plant Physiol., 90, 175, 1989
  • 17. I. Yruela, J.J. Pueyo, P.J. Alonso, R. Picorel, J. Biol. Chem., 271, 27408, 1996
  • 18. K. Burda, J. Kruk, G.H. Schmid, K. Strzalka, Biochem. J., 371, 597, 2003
  • 19. K. Burda, J. Kruk, R. Borgstädt, J. Stanek, K. Strzalka, G.H. Schmid, O. Kruse, FEBS Lett., 535, 159, 2003
  • 20. E.H. Haris, The Chlamydomonas Sourcebook, Academic Press, San Diego, CA 1989, p. 576
  • 21. V. Petrouleas, B.A. Diner, Biochim. Biophys. Acta, 849, 264, 1986
  • 22. B.A. Diner, F.A. Wollman, Eur. J. Biochem., 110, 521, 1980
  • 23. Ch. Andronis, O. Kruse, Z. Deak, I. Vass, B.A. Diner, J. Nixon, Plant. Physiol., 117, 515, 1998
  • 24. B.A. Diner, V. Petrouleas, Biochim. Biophys. Acta, 899, 138, 1987
  • 25. J. Kurreck, A. Garbers, F. Parak, G. Renger, FEBS Lett., 403, 283, 1997
  • 26. J. Kurreck, A. Garbers, F. Reiforth, L.E. Andreasson, F. Parak, G. Renger, FEBS Lett., 381, 53, 1996
  • 27. M. Roncel, J.M. Ortega, M. Losada, Eur. J. Biochem., 268, 4961, 2001
  • 28. G.T. Babcock, W.R. Widger, W.A. Cramer, W.A. Oerthing, J.G. Metz, Biochemistry, 24, 3638, 1985
  • 29. W.A. Cramer, G.-S. Tae, P.N. Furbacher, M. Bötter, Physiol. Plantarum, 88, 705, 1993
  • 30. M. Bernal, M. Roncel, J.M. Ortega, R. Picorel, I. Yruela, Physiol. Plantarum, 120, 686, 2004
  • 31. R. Fiege, U. Schreiber, G. Renger, W. Lubitz, V.A. Shuvalov, FEBS Lett., 377, 325, 1995
  • 32. R. Fiege, V.A. Shuvalov, FEBS Lett., 387, 33, 1996
  • 33. R.J. Hulsebosch, A.J. Hoff, V.A. Shuvalov, Biochim. Biophys. Acta, 1277, 103, 1996
  • 34. T.N. Kropacheva, W.O. Feikema, F. Mamedor, Y. Fryziger, S. Styring, A.J. Hoff, Chem. Phys., 294, 471, 2003
  • 35. S. Okayama, in: Proc. Int. Symp. on Photosynthetic Water Oxidation and Photosystem II Photochemistry, Eds. Y. Inoue, N. Murata, A.R. Crofts, G. Renger, Govindjee, K. Satoh, Academic Press, New York 1992, p. 393
  • 36. J. Kruk, K. Burda, A. Radunz, G.H. Schmid, K. Strzalka, Z. Naturforsch. C, 52, 766, 1997
  • 37. J. Kruk, K. Strzalka, J. Biol. Chem., 276, 86, 2001
  • 38. J. Kruk, G.H. Schmid, K. Strzalka, Plant Physiol. Biochem., 38, 271, 2000
  • 39. D.J. Arnon, G.M.S. Tang, Proc. Natl. Acad. Sci. USA, 85, 9524, 1988
  • 40. G. Renger, H.M. Gleiter, E. Haag, F. Reifarth, Z. Naturforsch. C, 48, 234, 1993
  • 41. L.M. Utschig, O. Poluektov, D.M. Tiede, M.C. Thurnauer, Biochemistry, 39, 2961, 2000
  • 42. V.V. Klimov, E. Dolan, E.R. Shaw, B. Ke, Proc. Natl. Acad. Sci. USA, 77, 7227, 1980
  • 43. R.J. Debus, G. Feher, M.Y. Okamura, Biochemistry, 25, 2276, 1986
  • 44. F. MacMillan, F. Ledzian, G. Renger, W. Lubitz, Biochemistry, 34, 8144, 1995
  • 45. H. Komiya, T.O. Hates, D.C. Rees, J.P. Allen, G. Feher, Proc. Natl. Acad. Sci. USA, 85, 9012, 1988
  • 46. Y. Sanakis, V. Petrouleas, B.A. Diner, Biochemistry, 33, 9922, 1994
  • 47. G.Ch. Dismukes, H.A. Frank, R. Freisner, K. Sauer, Biochim. Biophys. Acta, 764, 259, 1984
  • 48. V. Petrouleas, B.A. Diner, FEBS Lett., 147, 111, 1982
  • 49. V. Petrouleas, B.A. Diner, Biochim. Biophys. Acta, 893, 126, 1987
  • 50. B.A. Diner, V. Petrouleas, Biochim. Biophys. Acta, 1015, 141, 1990
  • 51. K.N. Ferreira, T.M. Irerson, K. Maghlaoni, J. Barber, S. Iwata, Science, 303, 1831, 2004
  • 52. A. Trebst, Z. Naturforsch. C, 42, 742, 1986
  • 53. D. Kouloughotis, T. Kostopoulos, V. Petrouleas, B.A. Diner, Biochim. Biophys. Acta, 1141, 275, 1993
  • 54. L. Rulisek, Z. Havlas, J. Am. Chem. Soc., 122, 10428, 2000
Document Type
Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-appv109n301kz
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