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The crystal structure of Escherichia coli bacterioferritin has been solved to 1.9 A, and shows the symmetrical binding of a haem molecule on the local twofold axis between subunits and a pair of metal atoms bound to each subunit at the ferroxidase centre. These metals have been identified as zinc by the analysis of the structure and X-ray data and confirmed by microfocused proton-induced X-ray emission experiments. For the first time the haem has been shown to be linked to both the internal and the external environments via a cluster of waters positioned above the haem molecule.

Original publication

DOI

10.1007/s00775-008-0438-8

Type

Journal article

Journal

J Biol Inorg Chem

Publication Date

02/2009

Volume

14

Pages

201 - 207

Keywords

Bacterial Proteins, Binding Sites, Ceruloplasmin, Crystallography, X-Ray, Cytochrome b Group, Escherichia coli, Ferritins, Heme, Models, Molecular, Molecular Structure, Protein Conformation, Zinc