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

Kashyap, Sanjay; Woehl, Taylor; Valverde-Tercedor, Carmen; Sánchez-Quesada, Miguel; Jiménez López, Concepción; Prozorov, Tanya

doi:10.1155/2014/320124

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

Journal Article · Wed Jan 01 00:00:00 EST 2014 · Journal of Nanomaterials

DOI:https://doi.org/10.1155/2014/320124· OSTI ID:1227740

Kashyap, Sanjay ^[1]; Woehl, Taylor ^[1];

^[2]; Sánchez-Quesada, Miguel ^[2]; Jiménez López, Concepción ^[2];

^[1]

Ames Laboratory, U.S. Department of Energy, Ames, IA 50011, USA
Department of Microbiology, University of Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain

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.

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Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-07CH11358; CGL2010-18274

OSTI ID:: 1227740

Journal Information:: Journal of Nanomaterials, Journal Name: Journal of Nanomaterials Vol. 2014; ISSN 1687-4110

Publisher:: Hindawi Publishing CorporationCopyright Statement

Country of Publication:: Egypt

Language:: English

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Cited by: 26 works

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