Table of Contents
ISRN Biophysics
Volume 2012 (2012), Article ID 124803, 5 pages
http://dx.doi.org/10.5402/2012/124803
Research Article

Density Functional Theory Study on Metal-Binding Energies for Human Serum Transferrin-Metal Complexes

1Faculty of Nutritional Sciences, The University of Morioka, Takizawa, Iwate 020-0183, Japan
2Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, 1–3 Kagurazaka, Shinjyuku-ku, Tokyo 162-8601, Japan

Received 16 December 2011; Accepted 3 January 2012

Academic Editors: D. Bulone and P. G. Fajer

Copyright © 2012 Tetsuya Sakajiri 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. J. H. Brock, Transferrins, Macmillan, London, UK, 1985.
  2. J. Wally, P. J. Halbrooks, C. Vonrhein et al., “The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding,” Journal of Biological Chemistry, vol. 281, no. 34, pp. 24934–24944, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. R. T. A. MacGillivray, S. A. Moore, J. Chen et al., “Two high-resolution crytal sructures of the recombinant N-lobe of human tranferrin reveal a structure change implicated in iron release,” Biochemistry, vol. 37, no. 22, pp. 7919–7928, 1998. View at Publisher · View at Google Scholar · View at Scopus
  4. D. R. Hall, J. M. Hadden, G. A. Leonard et al., “The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 Å, respectively,” Acta Crystallographica Section D, vol. 58, no. 1, pp. 70–80, 2002. View at Publisher · View at Google Scholar · View at Scopus
  5. W. R. Harris, Binding and Transport of Nonferrous Metals by Serum Transferrin, Springer, Berlin, Germany, 1998.
  6. H. Sun, H. Li, and P. J. Sadler, “Transferrin as a metal ion mediator,” Chemical Reviews, vol. 99, no. 9, pp. 2817–2842, 1999. View at Google Scholar · View at Scopus
  7. A. Dautry Varsat, A. Ciechanover, and H. F. Lodish, “pH and the recycling of transferrin during receptor-mediated endocytosis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 80, no. 8, pp. 2258–2262, 1983. View at Google Scholar · View at Scopus
  8. C. Harding, J. Heuser, and P. Stahl, “Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes,” Journal of Cell Biology, vol. 97, no. 2, pp. 329–339, 1983. View at Google Scholar · View at Scopus
  9. M. W. Hentze, M. U. Muckenthaler, B. Galy, and C. Camaschella, “Two to tango: regulation of mammalian iron metabolism,” Cell, vol. 142, no. 1, pp. 24–38, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. T. Yamamura, K. Ichimura, T. Tsuda et al., “Lanthanoid complex of iron-transport protein, transferrin—kinetic study on release of the metal from N and C binding sites,” Nippon Kagaku Kaishi, vol. 4, pp. 452–458, 1988. View at Google Scholar
  11. N. T. Ha-Duong, M. Hémadi, Z. Chikh, and J. M. E. H. Chahine, “Kinetics and thermodynamics of metal-loaded transferrins: transferrin receptor 1 interactions,” Biochemical Society Transactions, vol. 36, no. 6, pp. 1422–1426, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Sakajiri, T. Yamamura, T. Kikuchi, and H. Yajima, “Computational structure models of apo and diferric transferrin-transferrin receptor complexes,” Protein Journal, vol. 28, no. 9-10, pp. 407–414, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. T. Sakajiri, T. Yamamura, T. Kikuchi, K. Ichimura, T. Sawada, and H. Yajima, “Absence of binding between the human transferrin receptor and the transferrin complex of biological toxic trace element, aluminum, because of an incomplete open/closed form of the complex,” Biological Trace Element Research, vol. 136, no. 3, pp. 279–286, 2010. View at Publisher · View at Google Scholar · View at Scopus
  14. J. V. Princiotto and E. J. Zapolski, “Difference between the two iron binding sites of transferrin,” Nature, vol. 255, no. 5503, pp. 87–88, 1975. View at Google Scholar · View at Scopus
  15. T. A. D. Smith, “Human serum transferrin cobalt complex: stability and cellular uptake of cobalt,” Bioorganic and Medicinal Chemistry, vol. 13, no. 14, pp. 4576–4579, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. M. Hémadi, G. Miquel, P. H. Kahn, and J. M. El Hage Chahine, “Aluminum exchange between citrate and human serum transferrin and interaction with transferrin receptor 1,” Biochemistry, vol. 42, no. 10, pp. 3120–3130, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. L. R. Bernstein, “Mechanisms of therapeutic activity for gallium,” Pharmacological Reviews, vol. 50, no. 4, pp. 665–682, 1998. View at Google Scholar · View at Scopus
  18. W. W. Shreeve, “Use of isotopes in the diagnosis of hematopoietic disorders,” Experimental Hematology, vol. 35, no. 4, pp. 173–179, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. M. J. Frisch, G. W. Trucks, H. B. Schlegel et al., Gaussian03, in: C. Revisions C.01, D.02, and E.01, Ed, Gaussian, Inc., Wallingford, 2004.
  20. J. B. Foresman, T. A. Keith, K. B. Wiberg, J. Snoonian, and M. J. Frisch, “Solvent effects—5. Influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations,” Journal of Physical Chemistry, vol. 100, no. 40, pp. 16098–16104, 1996. View at Google Scholar · View at Scopus