skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Iron(III) clusters bound to horse spleen apoferritin: an X-ray absorption and Moessbauer spectroscopy study that shows that iron nuclei can form on the protein

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00376a023· OSTI ID:6521688

Ferritin is a complex of a hollow, spherical protein and a hydrous, ferric oxide core of less than or equal to4500 iron atoms inside the apoprotein coat; the apoprotein has multiple binding sites for monoatomic metal ions, e.g., Fe(II), V(IV), Tb(III), that may be important in the initiation of iron core formation. In an earlier study the authors observed that the oxidation of Fe(II) vacated some, but not all, of the metal-binding sites, suggesting migration of some Fe during oxidation, possibly to form nucleation clusters; some Fe(III) remained bound to the protein. Preliminary extended X-ray absorbance fine structure (EXAFS) analysis of the same Fe(III)-apoferritin complex showed an environment distinct from ferritin cores, but the data did not allow a test of the Fe cluster hypothesis. In this paper, with improved EXAFS data and with Moessbauer data on the same complex formed with /sup 57/Fe, they clearly show that the Fe(III) in the distinctive environment is polynuclear. Moreover, the arrangement of atoms is such that Fe(III) atoms appear to have both carboxylate-like ligands, presumably from apoferritin, and oxo bridges to the other iron atoms. Thus the protein provides sites not only for initiation but also for nucleation of the iron core. Sites commodious enough and with sufficient conserved carboxylate ligands to accommodate such a nucleus occur inside the protein coat at the subunit dimer interfaces. Such Fe(III)-apoferritin nucleation complexes can be used to study the properties of the several members of the apoferritin family.

Research Organization:
North Carolina State Univ., Raleigh
OSTI ID:
6521688
Journal Information:
Biochemistry; (United States), Vol. 26:2
Country of Publication:
United States
Language:
English