Staniland, S.S. and Rawlings, A.E. (2016) Crystallizing the function of the magnetosome membrane mineralization protein Mms6. Biochemical Society Transactions, 44 (3). pp. 883-890. ISSN 0300-5127
Abstract
The literature on the magnetosome membrane (MM) protein, magnetosome membrane specific6 (Mms6), is reviewed. Mms6 is native to magnetotactic bacteria (MTB). These bacteria take up iron from solution and biomineralize magnetite nanoparticles within organelles called magnetosomes. Mms6 is a small protein embedded on the interior of the MM and was discovered tightly associated with the formed mineral. It has been the subject of intensive research as it is seen to control the formation of particles both in vivo and in vitro. Here, we compile, review and discuss the research detailing Mms6’s activity within the cell and in a range of chemical in vitro methods where Mms6 has a marked effect on the composition, size and distribution of synthetic particles, with approximately 21 nm in size for solution precipitations and approximately 90 nm for those formed on surfaces. Furthermore, we review and discuss recent work detailing the structure and function of Mms6. From the evidence, we propose a mechanism for its function as a specific magnetite nucleation protein and summaries the key features for this action: namely, self-assembly to display a charged surface for specific iron binding, with the curvature of the surfaces determining the particle size. We suggest these may aid design of biomimetic additives for future green nanoparticle production.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY). |
Keywords: | iron-binding protein; magnetite nucleation; magnetosome; magnetotactic bacteria; membrane protein; Mms6 |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Funding Information: | Funder Grant number BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL (BBSRC) BB/H005412/2 |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 06 Jul 2016 08:29 |
Last Modified: | 06 Jul 2016 08:29 |
Published Version: | http://dx.doi.org/10.1042/BST20160057 |
Status: | Published |
Publisher: | Portland Press |
Refereed: | Yes |
Identification Number: | 10.1042/BST20160057 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:101603 |