Biological iron-sulfur storage in a thioferrateprotein nanoparticle
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 av...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Journal Article |
| Published: |
Macmillan Publishers Limited
2017
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| Online Access: | http://hdl.handle.net/20.500.11937/56250 |
| _version_ | 1848759825556570112 |
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| author | Vaccaro, B. Clarkson, S. Holden, J. Lee, D. Wu, C. Poole, F. Cotelesage, J. Hackett, Mark Mohebbi, S. Sun, J. Li, H. Johnson, M. George, G. Adams, M. |
| author_facet | Vaccaro, B. Clarkson, S. Holden, J. Lee, D. Wu, C. Poole, F. Cotelesage, J. Hackett, Mark Mohebbi, S. Sun, J. Li, H. Johnson, M. George, G. Adams, M. |
| author_sort | Vaccaro, B. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T10:06:02Z |
| format | Journal Article |
| id | curtin-20.500.11937-56250 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T10:06:02Z |
| publishDate | 2017 |
| publisher | Macmillan Publishers Limited |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-562502017-09-13T16:11:12Z Biological iron-sulfur storage in a thioferrateprotein nanoparticle Vaccaro, B. Clarkson, S. Holden, J. Lee, D. Wu, C. Poole, F. Cotelesage, J. Hackett, Mark Mohebbi, S. Sun, J. Li, H. Johnson, M. George, G. Adams, M. 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. 2017 Journal Article http://hdl.handle.net/20.500.11937/56250 10.1038/ncomms16110 Macmillan Publishers Limited unknown |
| spellingShingle | Vaccaro, B. Clarkson, S. Holden, J. Lee, D. Wu, C. Poole, F. Cotelesage, J. Hackett, Mark Mohebbi, S. Sun, J. Li, H. Johnson, M. George, G. Adams, M. Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title | Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title_full | Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title_fullStr | Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title_full_unstemmed | Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title_short | Biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| title_sort | biological iron-sulfur storage in a thioferrateprotein nanoparticle |
| url | http://hdl.handle.net/20.500.11937/56250 |