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Controlled formation of magnetite particles by Mms6

Mms6 represents a class of proteins that are tightly associated with the bacterial magnetite surface in M. magneticum AMB-1. The amino acid sequence of this protein is amphiphilic, and consists of an N-terminal LG-rich hydrophobic region and a C-terminal hydrophilic region containing multiplets of acidic amino acids. Following competitive iron binding analysis with other inorganic cations, it has been suggested that the C-terminal region is an iron binding site. Furthermore, this protein has previously shown iron binding activity, allowing it to generate uniform magnetic crystals by co-precipitation of ferrous and ferric ions. However, the exact role of Mms6 in the magnetite synthesis process still remains unknown. We have recently examined magnetite synthesis by a partial oxidation of ferrous hydroxide with and without the addition of Mms6, and their crystallographic characteristics were analyzed and compared. Mms6-mediated synthesis of magnetite by this method produced crystals of a uniform size and narrow size distribution with a cubooctahedral morphology, similar to bacterial magnetite observed in M. magneticum AMB-1. The crystals formed in the absence of Mms6 were octahedral, larger with an increased size distribution. The method presents an alternative route for controlling the size and shape of magnetite crystals without the use of organic solvent and high temperatures.