Abstract
Two copper(II)-ACC complexes were prepared and characterized: [Cu(bpy)(ACC)(
Two copper(II)-ACC complexes were prepared and characterized: [Cu(bpy)(ACC)(
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 Site | Google ScholarA. 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 Site | Google ScholarZ. 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 Site | Google ScholarA. 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 Site | Google ScholarD. 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 Site | Google ScholarJ. 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 activation in the biosynthesis of ethylene,” Journal of the American Chemical Society, vol. 124, no. 17, pp. 4602–4609, 2002.
View at: Publisher Site | Google ScholarA. 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 Site | Google ScholarM. 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 Site | Google ScholarR. 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 Site | Google ScholarJ. 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 Site | Google ScholarY. 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 Site | Google ScholarT. 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 ScholarF. 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 Site | Google ScholarW. 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 Site | Google ScholarN. 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 Site | Google ScholarA. 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 ScholarM. C. Pirrung, “Ethylene biosynthesis. 8. Structural and theoretical studies,” Journal of Organic Chemistry, vol. 52, no. 19, pp. 4179–4184, 1987.
View at: Publisher Site | Google ScholarG. 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 ScholarK. 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 Site | Google ScholarK. 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 -phosphate,” Inorganica Chimica Acta, vol. 186, no. 2, pp. 253–261, 1991.
View at: Publisher Site | Google ScholarW. Ghattas et al., unpublished results.
P. Capdevielle and M. Maumy, “A new oxidizing copper reagent : preparation and preliminary study of reactivity,” Tetrahedron Letters, vol. 31, no. 27, pp. 3891–3892, 1990.
View at: Publisher Site | Google ScholarL. 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 Site | Google ScholarJ. 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 Site | Google ScholarJ. 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 Site | Google ScholarB. 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 Site | Google ScholarM. 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 Site | Google ScholarI. 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 Site | Google Scholar