Direct observation of the iron binding sites in a ferritin

P D Hempstead; A J Hudson; P J Artymiuk; S C Andrews; M J Banfield; J R Guest; P M Harrison

doi:10.1016/0014-5793(94)00781-0

Direct observation of the iron binding sites in a ferritin

FEBS Lett. 1994 Aug 22;350(2-3):258-62. doi: 10.1016/0014-5793(94)00781-0.

Authors

P D Hempstead¹, A J Hudson, P J Artymiuk, S C Andrews, M J Banfield, J R Guest, P M Harrison

Affiliation

¹ Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.

PMID: 8070575
DOI: 10.1016/0014-5793(94)00781-0

Abstract

X-Ray analysis of the ferritin of Escherichia coli (Ec-FTN) and of Ec-FTN crystals soaked in (NH4)2Fe(SO4)2 has revealed the presence of three iron-binding sites per subunit. Two of these form a di-iron site in the centre of the subunit as has been proposed for the 'ferroxidase centres' of human ferritin H chains. This di-iron site, lying within the 4-alpha-helix bundle, resemble those of ribonucleotide reductase, methane monoxygenase and haemerythrin. The third iron is bound by ligands unique to Ec-FTN on the inner surface of the protein shell. It is speculated that this state may represent the nucleation centre of a novel type of Fe(III) cluster, recently observed in Ec-FTN.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry
Binding Sites
Crystallography, X-Ray
Escherichia coli
Ferritins / metabolism
Ferritins / ultrastructure*
Iron / metabolism*
Models, Molecular
Protein Structure, Tertiary

Substances

Bacterial Proteins
Ferritins
Iron