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Visualization of Iron‐Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC

Journal Article · · Journal of Nanomaterials
DOI:https://doi.org/10.1155/2014/320124· OSTI ID:1227740

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.

Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
AC02-07CH11358
OSTI ID:
1227740
Alternate ID(s):
OSTI ID: 1134614
Journal Information:
Journal of Nanomaterials, Journal Name: Journal of Nanomaterials Journal Issue: 1 Vol. 2014; ISSN 1687-4110
Publisher:
Hindawi Publishing CorporationCopyright Statement
Country of Publication:
Egypt
Language:
English

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