Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC
Abstract
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:
-
- 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
- Publication Date:
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1227740
- Grant/Contract Number:
- AC02-07CH11358; CGL2010-18274
- Resource Type:
- Published Article
- Journal Name:
- Journal of Nanomaterials
- Additional Journal Information:
- Journal Name: Journal of Nanomaterials Journal Volume: 2014; Journal ID: ISSN 1687-4110
- Publisher:
- Hindawi Publishing Corporation
- Country of Publication:
- Egypt
- Language:
- English
Citation Formats
Kashyap, Sanjay, Woehl, Taylor, Valverde-Tercedor, Carmen, Sánchez-Quesada, Miguel, Jiménez López, Concepción, and Prozorov, Tanya. Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC. Egypt: N. p., 2014.
Web. doi:10.1155/2014/320124.
Kashyap, Sanjay, Woehl, Taylor, Valverde-Tercedor, Carmen, Sánchez-Quesada, Miguel, Jiménez López, Concepción, & Prozorov, Tanya. Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC. Egypt. https://doi.org/10.1155/2014/320124
Kashyap, Sanjay, Woehl, Taylor, Valverde-Tercedor, Carmen, Sánchez-Quesada, Miguel, Jiménez López, Concepción, and Prozorov, Tanya. Wed .
"Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC". Egypt. https://doi.org/10.1155/2014/320124.
@article{osti_1227740,
title = {Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC},
author = {Kashyap, Sanjay and Woehl, Taylor and Valverde-Tercedor, Carmen and Sánchez-Quesada, Miguel and Jiménez López, Concepción and Prozorov, Tanya},
abstractNote = {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.},
doi = {10.1155/2014/320124},
journal = {Journal of Nanomaterials},
number = ,
volume = 2014,
place = {Egypt},
year = {Wed Jan 01 00:00:00 EST 2014},
month = {Wed Jan 01 00:00:00 EST 2014}
}
https://doi.org/10.1155/2014/320124
Web of Science
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