Abstract
Iron is a precious metal for the organism because of its unsurpassed versatility as a biological catalyst. It is involved in a broad spectrum of essential biological functions such as oxygen transport (hemoglobin), electron transfer (mitochondrial heme and non-heme Fe proteins essential for energy production) and DNA synthesis (ribonucleotide reductase), to name just a few. However, the chemical properties of iron which allow this versatility also lead to the paradoxical situation that acquisition by the organism of an abundant element is exceedingly difficult. At pH 7.4 and physiological oxygen tension, the relatively soluble ferrous ion (Fe2+) is readily oxidized to ferric ion (Fe3+) which is susceptible to hydrolysis, forming virtually insoluble ferric hydroxides. The concentration of aquated Fe3+ (pH 7.4) cannot exceed 10-17 M. Moreover, unless bound to specific ligands, iron plays a key role in the formation of harmful oxygen radicals which ultimately cause oxidative damage to vital cell structures. Because of this virtual insolubility and potential toxicity, specialized mechanisms and molecules for the acquisition, transport, and storage of iron in a soluble nontoxic form have evolved to meet cellular and organismal iron requirements. In addition, organisms are equipped with sophisticated mechanisms that prevent the expansion of the catalytically active intracellular iron pool, while maintaining sufficient concentrations of the metal for metabolic use.1–3 However, despite these homeostatic mechanisms, organisms often face the threat of either iron deficiency or iron overload.
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Buss, J.L., Hermes-Lima, M., Ponka, P. (2002). Pyridoxal Isonicotinoyl hydrazone and its analogues. In: Hershko, C. (eds) Iron Chelation Therapy. Advances in Experimental Medicine and Biology, vol 509. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0593-8_11
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