The ferritin family of iron storage proteins - PubMed (original) (raw)

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The ferritin family of iron storage proteins

E C Theil. Adv Enzymol Relat Areas Mol Biol. 1990.

Abstract

The ferritins are a family of proteins produced in a variety of amounts and types depending on the state of development of an animal, or the state of differentiation of a particular cell type, or the environment. Iron storage is the main function of the ferritins when iron is needed for intracellular use (housekeeping) for iron proteins such as ribonucleotide reductase, cytochromes, oxidases, nitrogenases, or photosynthetic reaction centers or for extracellular use by other cells (specialized). Under abnormal conditions, such as the breach of transferrin-receptor-controlled incorporation of iron, ferritin can also serve to detoxify excess intracellular iron. The structure of ferritin is very complex, consisting of a protein coat of 24 polypeptide subunits, approximately 20 kDa, which surrounds an inorganic phase of hydrous ferric oxide. The polypeptide subunits, bundles of four alpha helices, display remarkable conservation of sequence among plants and animals, which is probably related to the necessity of forming the hollow sphere pierced by 14 channels through which iron may pass. In spite of the conserved regions of sequence, there are multiple genes for ferritin polypeptide subunits within an organism; at the moment three distinct subunit types, H H'(or M), and L, have been identified which are expressed in a cell-specific fashion. How many different subunit types exist, the influence on function, and the number of genes required to encode them are currently being actively investigated. Not only does the protein coat of ferritin display variations, the inorganic phase of ferritin can vary as well. For instance, differences can occur in the number of Fe atoms (up to 4500), as well as in the phosphorus content and in the degree of hydration and order. Such observations have depended on the use of a variety of physical techniques such as X-ray diffraction, EXAFS, and Mössbauer spectroscopy. The same approaches, as well as EPR spectroscopy, have been used to monitor the path taken by Fe as it passes from mononuclear Fe(II) outside the protein coat to polynuclear Fe(III) inside the protein coat. Both mononuclear Fe(II) and Fe(III) have been observed, as well as dimeric Fe(II)-O-Fe(III), and Fe(III)-oxo bridged clusters attached to the protein. A possible protein site for the Fe(III) cluster is a groove on the inner surface of the dimeric interface, suggested by the structure and from the affect of natural cross-links between subunit pairs.(ABSTRACT TRUNCATED AT 400 WORDS)

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