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The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin.

J. Biol. Inorg. Chem.2009 Feb;14(2):201-7. doi:10.1007/s00775-008-0438-8. Epub 2008 Oct 23
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摘要


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.

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