Iron transport and storage proteins

There are many other proteins that contain iron in a form that is neither in haem nor in iron-sulfur clusters. We have already encountered the iron storage and transport proteins, ferritin and transferrin (see Chapter 8). We propose to discuss here two other classes of iron-containing proteins, those with mononuclear non-haem iron centres and those with dinuclear non-haem iron centres. 

The relevant biological questions are how the iron is converted from mineral to protein and once in the protein what is the specialized role played by the iron in the function of that protein In this chapter we concern ourselves with the means by which iron is obtained and secured for the living organism through the iron storage and transport proteins, and in particular how Mossbauer effect and electron spin resonance spectroscopy can help to understand the electronic and molecular structure of these proteins. 

Antanaitis, B., Aisen, P. in Urushizaki, I., Aisen, P., Listowsky, I., Drysdale, J. (eds.) Structure and Function of Iron Storage and Transport Proteins, Elsevier, Amsterdam (1983)... 

Peters, S.W., Jones, B.M., Jacobs, A. and Wagstaff, M. (1985). Free iron and lipid peroxidation in the plasma of patients with iron overload. In Proteins of Iron Storage and Transport (eds. G. Spik, J. Montreuil, R.R. Crichton and J. Mazurier) pp. 321-324. Elsevier Science Publishers, New York. 

Neuwirt, J., Borova, J. Pohka, P., Proteins of Iron Storage and Transport... 

Proteins of Iron Storage and Transport in Biology and Medicine, R. R. Crichton, Ed., pp. 39-50, North Holland, Amsterdam, 1975. 

Spik, G., Montreuil, J., Crichton, R.R. and Mazurier, J. (1985), Proteins of Iron Storage and Transport, Proc. 7th Intern. Conference on Proteins of Iron Metabolism, Villeneuve d Ascq (France), 30 June-5 July 1985. Elsevier, Amsterdam. 

Redox-active metal ions are present in the cell in their free, uncomplexed state only in extremely low concentrations. They are instead sequestered by metal-ion storage and transport proteins, such as ferritin and transferrin for iron (see Chapter 1) and ceruloplasmin for copper. This arrangement prevents such metal ions from catalyzing deleterious oxidative reactions, but makes them available for incorporation into metalloenzymes as they are needed. 

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