Biological iron-sulfur storage in a thioferrateprotein nanoparticle
|dc.identifier.citation||Vaccaro, B. and Clarkson, S. and Holden, J. and Lee, D. and Wu, C. and Poole, F. and Cotelesage, J. et al. 2017. Biological iron-sulfur storage in a thioferrateprotein nanoparticle. Nature Communications. 8.|
Iron-sulfur clusters are ubiquitous in biology and function in electron transfer and catalysis. They are assembled from iron and cysteine sulfur on protein scaffolds. Iron is typically stored as iron oxyhydroxide, ferrihydrite, encapsulated in 12 nm shells of ferritin, which buffers cellular iron availability. Here we have characterized IssA, a protein that stores iron and sulfur as thioferrate, an inorganic anionic polymer previously unknown in biology. IssA forms nanoparticles reaching 300 nm in diameter and is the largest natural metalloprotein complex known. It is a member of a widely distributed protein family that includes nitrogenase maturation factors, NifB and NifX. IssA nanoparticles are visible by electron microscopy as electron-dense bodies in the cytoplasm. Purified nanoparticles appear to be generated from 20 nm units containing ~6,400 Fe atoms and ~170 IssA monomers. In support of roles in both iron-sulfur storage and cluster biosynthesis, IssA reconstitutes the [4Fe-4S] cluster in ferredoxin in vitro.
|dc.publisher||Macmillan Publishers Limited|
|dc.title||Biological iron-sulfur storage in a thioferrateprotein nanoparticle|
|curtin.department||Department of Chemistry|
|curtin.accessStatus||Open access via publisher|
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