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Bovine aconitase showing FeS4 cluster complex with sulfate (PDB code 1amj)

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  • M. Claire Kennedy and Helmut Beinert: IX.4. Aconitase. in Ivano Bertini, Harry B. Gray, Edward I. Stiefel, Joan Selverstone Valentine (eds.): Biological Inorganic Chemistry: Structure and Reactivity. University Science Books, Herndon 2006. ISBN 1891389432 pp.209--

Additional Resources

For additional information, see: Carbohydrate Metabolism; Krebs cycle step 2.


  1. Zheng L, Kennedy MC, Beinert H, Zalkin H. Mutational analysis of active site residues in pig heart aconitase. J Biol Chem. 1992 Apr 15;267(11):7895-903. PMID:1313811
  2. 2.0 2.1 Frishman D, Hentze MW. Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationships. Eur J Biochem. 1996 Jul 1;239(1):197-200. PMID:8706708
  3. Dupuy J, Volbeda A, Carpentier P, Darnault C, Moulis JM, Fontecilla-Camps JC. Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure. 2006 Jan;14(1):129-39. PMID:16407072 doi:10.1016/j.str.2005.09.009
  4. 4.0 4.1 4.2 Beinert, H., Kennedy, M. C., Stout, C.D. “Aconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory Protein.” Chem. Rev. 1996, 96, 2335−2373.
  5. Lauble H, Kennedy MC, Beinert H, Stout CD. Crystal structures of aconitase with trans-aconitate and nitrocitrate bound. J Mol Biol. 1994 Apr 8;237(4):437-51. PMID:8151704 doi:
  6. 6.0 6.1 6.2 6.3 Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. p. 578-579. Print.
  7. 7.0 7.1 Flint, DH., and Allen, RM. "Iron-sulfur protein with nonredox functions.” Chem. Rev. 1996, 96, 2315−2334.

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