A bacterium reveals the crucible of its metallurgical activity

A bacterium reveals the crucible of its metallurgical activity

The determination of the structure of the protein MamP has shown for the first time that a section of this protein possesses an original folding structure known as a magnetochrome. This structure is only found in magnetotactic bacteria. The structure has a crucible-like shape capable of containing iron. Additional experiments have shown that MamP has the ability to oxidize iron from the Fe(II) state to the Fe(III) state, and to stabilize the latter in its crucible. Mutagenesis studies and the phenotyping of magnetotactic bacteria variants have confirmed the physiological importance of this crucible.

Finally, a number of in vitro experiments have shown that MamP is capable of producing a magnetite precursor when incubated in the presence of Fe(II) alone, proving that the Fe (III) results from the activity of this protein.

This fundamental study reveals part of the process whereby iron is biomineralized and nanomagnets are synthesized in magnetotactic bacteria. The potential applications of these nanomagnets appear promising. They may, for example, by used as a contrast agent in magnetic resonance imaging. Another possible application relates to the decontamination of water supplies. Magnetotactic bacteria carrying an enzyme that breaks down a contaminant may be used to treat effluent and may then easily be removed from the water by means of a magnet.

The work described in this study was partly funded by Eurotalent and supported by the Biomineralization and Nanostructure International Associated Laboratory.

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