Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC
Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC
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DOI：
10.1155/2014/320124
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发表时间：
2014-01-01
影响因子：
--
通讯作者：
Prozorov, Tanya
中科院分区：
文献类型：
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作者：
Kashyap, Sanjay;Woehl, Taylor;Prozorov, Tanya
低温合成方法利用生物大分子对纳米颗粒的成核和放置进行精确控制。它们能够在低温下形成各种功能纳米结构材料，这些材料的特性通常是通过传统合成技术无法实现的。本文报道了一种新的酸性细菌重组蛋白MamC的原位可视化，该蛋白通常存在于几种趋磁细菌的磁小体膜中，包括海洋磁球菌，菌株MC-1。我们的研究结果提供了对MamC自组装的深入了解，并指出了延伸蛋白表面的形成，这被认为在生物模板化无机纳米颗粒的形成中起着重要作用。MamC的自组织与另一种酸性重组铁结合蛋白Mms6的行为进行了比较。
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.