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Biomineralization by living organisms provides excellent examples of controlled mineral synthesis for us to learn how to produce materials with desired morphologies and properties under ambient conditions. Magnetotactic bacteria (MTBs) are an example of biomineralizing organisms that produce magnetic nanoparticles. MTBs are a diverse family of organisms that are capable of producing nano-sized magnetic particles inside the cell-body with finely controlled particle size and magnetic properties. A single protein, Mms6, from these bacteria was shown to direct the biomineralization of magnetite nanoparticles from iron solutions in vitro. Previous work showed that Mms6 forms micelles in solution, with the hydrophobic Nterminal domain incorporated in the micelle and C-terminal domain exposed on the surface of the micelle. Evidence was obtained for a structural change of Mms6 when it binds with Fe 3+ as shown by CD spectroscopy and by measuring intrinsic tryptophan fluorescence. But how the protein forms micelles and undergoes structural change upon contact with iron regulates the crystallization process was still to be determined. By using TEM and AFM microscopy, I visualized the spherical micelles formed by Mms6. The results reported in chapter 2 of this thesis are consistent with the view that the N and C-terminal domains interact with each other within one polypeptide chain and across protein units in the assembly. From protein mutational studies to determine the amino acid residues important for self-assembly, I identified the unique GL repeat in the N-terminal domain with additional contributions from amino acids in other positions, throughout the molecule. Analysis by CD spectroscopy identified a structural change in the iron-binding Cterminal domain in the presence of Fe 3+ . A change in the intrinsic fluorescence of tryptophan in the N-terminal domain showed that this structural change is transmitted through the

Self-assembly of biomineralization protein Mms6 and its function as a ferric iron reductase that associates with lipid membranes