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Bioinorganic Chemistry and Applications
Volume 2007 (2007), Article ID 43424, 9 pages
http://dx.doi.org/10.1155/2007/43424
Research Article

Characterization of Cu(II)-ACC Complexes and Conversion of the Bound ACC into Ethylene in the Presence of Hydrogen Peroxide. Detection of a Brown Intermediate at Low Temperature

1BiosCiences FRE CNRS 3005, Faculté des Sciences et Techniques, Université Paul Cézanne Aix-Marseille III, avenue Escadrille Normandie-Niémen, Marseille Cedex 20 13397, France
2Spectropôle, Faculté des Sciences et Techniques, Université Paul Cézanne Aix-Marseille III, avenue Escadrille Normandie-Niémen, Marseille Cedex 20 13397, France
3Central Research Institute for Chemistry, Hungarian Academy of Sciences, P.O. Box 17, Budapest 1525, Hungary

Received 26 March 2007; Accepted 16 July 2007

Academic Editor: Marc Fontecave

Copyright © 2007 Wadih Ghattas et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. P. John, “Ethylene biosynthesis: the role of 1-aminocyclopropane-1-carboxylate (ACC) oxidase, and its possible evolutionary origin,” Physiologia Plantarum, vol. 100, no. 3, pp. 583–592, 1997. View at Publisher · View at Google Scholar
  2. A. B. Bleecker and H. Kende, “Ethylene: a gaseous signal molecule in plant,” Annual Review of Cell and Developmental Biology, vol. 16, pp. 1–18, 2000. View at Publisher · View at Google Scholar
  3. Z. Zhang, J.-S. Ren, I. J. Clifton, and C. J. Schofield, “Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase—the ethylene-forming enzyme,” Chemistry & Biology, vol. 11, no. 10, pp. 1383–1394, 2004. View at Publisher · View at Google Scholar
  4. A. M. Rocklin, D. L. Tierney, V. Kofman et al., “Role of the nonheme Fe(II) center in the biosynthesis of the plant hormone ethylene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 14, pp. 7905–7909, 1999. View at Publisher · View at Google Scholar
  5. D. L. Tierney, A. M. Rocklin, J. D. Lipscomb, L. Que Jr., and B. M. Hoffman, “ENDOR studies of the ligation and structure of the non-heme iron site in ACC oxidase,” Journal of the American Chemical Society, vol. 127, no. 19, pp. 7005–7013, 2005. View at Publisher · View at Google Scholar
  6. J. Zhou, A. M. Rocklin, J. D. Lipscomb, L. Que Jr., and E. I. Solomon, “Spectroscopic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: molecular mechanism and CO2 activation in the biosynthesis of ethylene,” Journal of the American Chemical Society, vol. 124, no. 17, pp. 4602–4609, 2002. View at Publisher · View at Google Scholar
  7. A. M. Rocklin, K. Kato, H.-W. Liu, L. Que Jr., and J. D. Lipscomb, “Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction,” Journal of Biological Inorganic Chemistry, vol. 9, no. 2, pp. 171–182, 2004. View at Publisher · View at Google Scholar
  8. M. Costas, M. P. Mehn, M. P. Jensen, and L. Que Jr., “Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates,” Chemical Reviews, vol. 104, no. 2, pp. 939–986, 2004. View at Publisher · View at Google Scholar
  9. R. M. Adlington, J. E. Baldwin, and B. J. Rawlings, “On the stereochemistry of ethylene biosynthesis,” Journal of the Chemical Society, Chemical Communication, no. 6, pp. 290–292, 1983. View at Publisher · View at Google Scholar
  10. J. E. Baldwin, D. A. Jackson, R. M. Adlington, and B. J. Rawlings, “The stereochemistry of oxidation of 1-amino-cyclopropanecarboxylic acid,” Journal of the Chemical Society, Chemical Communication, no. 4, pp. 206–207, 1985. View at Publisher · View at Google Scholar
  11. Y. Nishida, T. Akamatsu, T. Ishii, and Y. Oda, “Evolution of ethylene from 1-aminocyclopropanecarboxylic acid by binuclear iron(III)-peroxide adducts,” Journal of the Chemical Society, Chemical Communications, no. 6, pp. 496–497, 1992. View at Publisher · View at Google Scholar
  12. T. Kobayashi, Y. Sasaki, T. Akamatsu et al., “Non-enzymatic RNA hydrolysis promoted by the combined catalytic activity of buffers and magnesium ions,” Zeitschrift für Naturforschung, vol. 54c, pp. 534–541, 1999. View at Google Scholar
  13. F. H. Allen, “The cambridge structural database: a quarter of a million crystal structures and rising,” Acta Crystallographica B, vol. 58, no. 1, part 3, pp. 380–388, 2002. View at Publisher · View at Google Scholar
  14. W. Ghattas, C. Gaudin, M. Giorgi, A. Rockenbauer, A. J. Simaan, and M. Réglier, “ACC-oxidase like activity of a copper (II)-ACC complex in the presence of hydrogen peroxide. Detection of a reaction intermediate at low temperature,” Chemical Communications, no. 9, pp. 1027–1029, 2006. View at Publisher · View at Google Scholar
  15. N. Judaš and N. Raos, “Self-assembly of cis and trans forms of the copper(II) complex with 1-aminocyclopropane-1-carboxylate into discrete trimers in the solid state,” Inorganic Chemistry, vol. 45, no. 13, pp. 4892–4894, 2006. View at Publisher · View at Google Scholar
  16. A. Rockenbauer and L. Korecz, “Automatic computer simulations of ESR spectra,” Applied Magnetic Resonance, vol. 10, no. 1–3, pp. 29–43, 1996. View at Google Scholar
  17. M. C. Pirrung, “Ethylene biosynthesis. 8. Structural and theoretical studies,” Journal of Organic Chemistry, vol. 52, no. 19, pp. 4179–4184, 1987. View at Publisher · View at Google Scholar
  18. G. Valle, M. Crisma, C. Toniolo et al., “Crystallographic characterization of conformation of 1-aminocyclopropane-1-carboxylic acid residue (Ac3c) in simple derivatives and peptides,” International Journal of Peptide and Protein Research, vol. 34, no. 1, pp. 56–65, 1989. View at Google Scholar
  19. K. Aoki and H. Yamazaki, “Crystal structure of the 1-aminocyclopropanecarboxylate—pyridoxal Schiff base complex of copper(II): a model for a Schiff base intermediate in ethylene biosynthesis,” Journal of the Chemical Society, Chemical Communication, no. 16, pp. 1241–1242, 1987. View at Publisher · View at Google Scholar
  20. K. Aoki, N. Hu, and H. Yamazaki, “X-ray studies on metal ion interactions with vitamins II. Crystal structures of three copper(II) and nickel(II) complexes of Schiff bases formed between 1-aminocyclopropanecarboxylic acid and pyridoxal or pyridoxal 5-phosphate,” Inorganica Chimica Acta, vol. 186, no. 2, pp. 253–261, 1991. View at Publisher · View at Google Scholar
  21. W. Ghattas et al., unpublished results.
  22. P. Capdevielle and M. Maumy, “A new oxidizing copper reagent : Cuα2H preparation and preliminary study of reactivity,” Tetrahedron Letters, vol. 31, no. 27, pp. 3891–3892, 1990. View at Publisher · View at Google Scholar
  23. L. M. Mirica, X. Ottenwaelder, and T. D. P. Stack, “Structure and spectroscopy of copper-dioxygen complexes,” Chemical Reviews, vol. 104, no. 2, pp. 1013–1046, 2004. View at Publisher · View at Google Scholar
  24. J. M. Dunwell, A. Purvis, and S. Khuri, “Cupins: the most functionally diverse protein superfamily?” Phytochemistry, vol. 65, no. 1, pp. 7–17, 2004. View at Publisher · View at Google Scholar
  25. J. M. Dunwell, A. Culham, C. E. Carter, C. R. Sosa-Aguirre, and P. W. Goodenough, “Evolution of functional diversity in the cupin superfamily,” Trends in Biochemical Sciences, vol. 26, no. 12, pp. 740–746, 2001. View at Publisher · View at Google Scholar
  26. B. M. Barney, M. R. Schaab, R. LoBrutto, and W. A. Francisco, “Evidence for a new metal in a known active site: purification and characterization of an iron-containing quercetin 2,3-dioxygenase from Bacillus subtilis,” Protein Expression and Purification, vol. 35, no. 1, pp. 131–141, 2004. View at Publisher · View at Google Scholar
  27. M. R. Schaab, B. M. Barney, and W. A. Francisco, “Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis,” Biochemistry, vol. 45, no. 3, pp. 1009–1016, 2006. View at Publisher · View at Google Scholar
  28. I. M. Kooter, R. A. Steiner, B. W. Dijkstra, P. I. van Noort, M. R. Egmond, and M. Huber, “EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates,” European Journal of Biochemistry, vol. 269, no. 12, pp. 2971–2979, 2002. View at Publisher · View at Google Scholar