Works Cited

  1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., and Lipman, D.J. (1990). Basic local alignment search tool (1990). J. Mol. Biol. 215:403-10.
  2. Garrett, R., and Grisham, C.M. (2013). The tricarboxylic acid cycle. Biochemistry. Belmont, CA: Brooks/Cole, Cengage Learning. 602-20. Print.
  3. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., and Bairoch A. (2005). Protein identification and analysis tools on the ExPASy Server. John M Walker (ed): The Proteomics Protocols Handbook. Humana Press. 571-607 
  4. Helmut, B., Kennedy, M.C., and Stout, C.D. (1996). Aconitase as iron−sulfur protein, enzyme, and iron-regulatory protein. Chemical Reviews. 7: 2335-374.
  5. Holm L., and Rosenstrom P. (2010). Dali server: conservation mapping in 3D. Nucl. Acids Res. 38, W545-549.
  6. Kabsch W., and Sander C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 12: 2577-637.
  7. Lauble, H., Kennedy, M.C., Beinert, H.,  and Stout, C.D. (1992). Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Biochemistry. 31: 2735-48.
  8. Lloyd, S. J., Lauble, H., Prasad, G. S. and Stout, C. D. (1999), The mechanism of aconitase: 1.8 Å resolution crystal structure of the S642A:citrate complex. Protein Science, 8: 2655–62.
  9. Robbins, A. H., and Stout, C.D. (1989). Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proceedings of the National Academy of Sciences. 86.10: 3639-43.
  10. Sigel, A., and H. Sigel. Ed. I. Bertini. Handbook on Metalloproteins. 2nd ed. N.p.: n.p., 2000. 389-90. Print.
  11. Zheng, L.,  Kennedy, M.C., Beinert, H., and Zalkin H.(1992). Mutational analysis of active site residues in pig heart aconitase. The Journal of Biological Chemistry 267.11: 7895-903.