Biological iron-sulfur storage in a thioferrateprotein nanoparticle

Brian J. Vaccaro, Sonya M. Clarkson, James F. Holden, Dong Woo Lee, Chang Hao Wu, Farris L. Poole, Julien J.H. Cotelesage, Mark J. Hackett, Sahel Mohebbi, Jingchuan Sun, Huilin Li, Michael K. Johnson, Graham N. George, Michael W.W. Adams

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number16110
JournalNature communications
Volume8
DOIs
Publication statusPublished - 2017 Jul 20

Fingerprint

Sulfur
Nanoparticles
sulfur
Iron
iron
nanoparticles
proteins
Metalloproteins
biology
Electrons
Iron-Sulfur Proteins
Nitrogenase
Ferredoxins
Biosynthesis
Ferritins
Catalysis
Scaffolds
Electron microscopy
Cysteine
biosynthesis

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Vaccaro, B. J., Clarkson, S. M., Holden, J. F., Lee, D. W., Wu, C. H., Poole, F. L., ... Adams, M. W. W. (2017). Biological iron-sulfur storage in a thioferrateprotein nanoparticle. Nature communications, 8, [16110]. https://doi.org/10.1038/ncomms16110
Vaccaro, Brian J. ; Clarkson, Sonya M. ; Holden, James F. ; Lee, Dong Woo ; Wu, Chang Hao ; Poole, Farris L. ; Cotelesage, Julien J.H. ; Hackett, Mark J. ; Mohebbi, Sahel ; Sun, Jingchuan ; Li, Huilin ; Johnson, Michael K. ; George, Graham N. ; Adams, Michael W.W. / Biological iron-sulfur storage in a thioferrateprotein nanoparticle. In: Nature communications. 2017 ; Vol. 8.
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Vaccaro, BJ, Clarkson, SM, Holden, JF, Lee, DW, Wu, CH, Poole, FL, Cotelesage, JJH, Hackett, MJ, Mohebbi, S, Sun, J, Li, H, Johnson, MK, George, GN & Adams, MWW 2017, 'Biological iron-sulfur storage in a thioferrateprotein nanoparticle', Nature communications, vol. 8, 16110. https://doi.org/10.1038/ncomms16110

Biological iron-sulfur storage in a thioferrateprotein nanoparticle. / Vaccaro, Brian J.; Clarkson, Sonya M.; Holden, James F.; Lee, Dong Woo; Wu, Chang Hao; Poole, Farris L.; Cotelesage, Julien J.H.; Hackett, Mark J.; Mohebbi, Sahel; Sun, Jingchuan; Li, Huilin; Johnson, Michael K.; George, Graham N.; Adams, Michael W.W.

In: Nature communications, Vol. 8, 16110, 20.07.2017.

Research output: Contribution to journalArticle

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T1 - Biological iron-sulfur storage in a thioferrateprotein nanoparticle

AU - Vaccaro, Brian J.

AU - Clarkson, Sonya M.

AU - Holden, James F.

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AU - Wu, Chang Hao

AU - Poole, Farris L.

AU - Cotelesage, Julien J.H.

AU - Hackett, Mark J.

AU - Mohebbi, Sahel

AU - Sun, Jingchuan

AU - Li, Huilin

AU - Johnson, Michael K.

AU - George, Graham N.

AU - Adams, Michael W.W.

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N2 - 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.

AB - 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.

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