References
- Neilands J. B. Evolution of biological iron binding centers. Structure and Bonding 1972; 11: 145–170
- Baker M. S., Gebicki J. M. The effect of pH on yields of hydroxyl radicals produced from superoxide by potential biological iron chelators. Archives of Biochemistry and Biophysics 1986; 246: 581–588
- Gutteridge J. M. C. Hydroxyl radical formation from the auto-reduction of a ferric citrate complex. Free Radical Biology and Medicine 1991; 11: 401–406
- Paraskeva E., Hentze M. W. Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. Federation of European Biochemical Societies Letters 1996; 389: 40–43
- Kennedy M. C., Emptage M. H., Dreyer J. L., Beinert H. The role of iron in the activation-inactivation of aconitase. The Journal of Biological Chemistry 1983; 258: 11098–11105
- Thiel E. C. Iron regulatory elements (IRES): a family of mRNA non-coding sequences. Biochemical Journal 1994; 304: 1–11
- Fujita T., Hamasak H., Fwukata C., Nonobe M. New enzymatic assay of iron in serum. Clinical Chemistry 1994; 40: 763–767
- Mumby S., Koizumi M., Taniguchi N., Gutteridge J. M. C. Reactive iron species in biological fluids activate the iron-sulphur cluster of aconitase. Biochimica et Biophysica Acta 1997, In press
- Gutteridge J. M. C., Mumby S., Koizumi M., Taniguchi N. “Free” iron in neonatal plasma activates aconitase: Evidence for biologically reactive iron. Biochemical and Biophysical Research Communications 1996; 229: 806–809