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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.
 [1] ;  [1] ;  [2] ;  [2] ;  [2] ;  [1]
  1. Ames Laboratory, U.S. Department of Energy, Ames, IA 50011, USA
  2. Department of Microbiology, University of Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain
Publication Date:
OSTI Identifier:
Grant/Contract Number:
AC02-07CH11358; CGL2010-18274
Published Article
Journal Name:
Journal of Nanomaterials
Additional Journal Information:
Journal Volume: 2014; Related Information: CHORUS Timestamp: 2016-08-18 12:53:27; Journal ID: ISSN 1687-4110
Hindawi Publishing Corporation
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication: