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Title: Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC

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.
Authors:
 [1] ;  [1] ;  [2] ;  [2] ;  [2] ;  [1]
  1. Ames Laboratory
  2. University of Granada
Publication Date:
OSTI Identifier:
1134614
Report Number(s):
IS-J 8234
Journal ID: ISSN 1687-4110
DOE Contract Number:
DE-AC02-07CH11358
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Nanomaterials; Journal Volume: 2014
Publisher:
Hindawi
Research Org:
Ames Laboratory (AMES), Ames, IA (United States)
Sponsoring Org:
USDOE Office of Science (SC)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE