Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC
- Ames Laboratory
- University of Granada
Biological macromolecules are utilized in low-temperature synthetic methods to exert precise control over nanoparticle nucleation and placement. They enable low-temperature formation of a variety of functional nanostructured materials with properties often not achieved via conventional synthetic techniques. Here we report on the in situ visualization of a novel acidic bacterial recombinant protein, MamC, commonly present in the magnetosome membrane of several magnetotactic bacteria, including Magnetococcus marinus, strain MC-1. Our findings provide an insight into the self-assembly of MamC and point to formation of the extended protein surface, which is assumed to play an important role in the formation of biotemplated inorganic nanoparticles. The self-organization of MamC is compared to the behavior of another acidic recombinant iron-binding protein, Mms6.
- Research Organization:
- Ames Lab., Ames, IA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC)
- DOE Contract Number:
- DE-AC02-07CH11358
- OSTI ID:
- 1134614
- Report Number(s):
- IS-J 8234
- Journal Information:
- Journal of Nanomaterials, Vol. 2014; ISSN 1687-4110
- Publisher:
- Hindawi
- Country of Publication:
- United States
- Language:
- English
Similar Records
Subcellular localization of the magnetosome protein MamC in the marine magnetotactic bacterium Magnetococcus marinus strain MC-1 using immunoelectron microscopy
Isolation, cultivation and genomic analysis of magnetosome biomineralization genes of a new genus of South-seeking magnetotactic cocci within the Alphaproteobacteria