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Home / Equine Research Bank / Chemistry / Iron Biomineral Growth from the Initial Nucleation Seed in L...
Chemistry (Weinheim an der Bergstrasse, Germany)2020; 26(26); 5770-5773; doi: 10.1002/chem.202000064

Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin.

Abstract: X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner surface of the protein cage with a key role played by some glutamate residues. An atomic resolution view of how the cluster formation develops starting from a (μ -oxo)tris[(μ -glutamato-κO:κO')](glutamato-κO)(diaquo)triiron(III) seed is provided. The results support the idea that iron biomineralization in ferritin is a process initiating at the level of the protein surface, capable of contributing coordination bonds and electrostatic guidance.
© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Publication Date: 2020-03-31 PubMed ID: 32027764DOI: 10.1002/chem.202000064Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research study uses x-ray structures to explore how iron biomineralization in ferritin, a protein that stores and releases iron in the body, starts from a single triiron(III) seed and develops with the help of glutamate residues, eventually forming an octa-nuclear iron cluster.

Studying Iron Biomineralization in Ferritin

  • The research centers around the process of iron biomineralization in ferritin. This is the process through which ferritin, a protein that is responsible for storing and releasing iron within the body, forms an iron mineral cluster.
  • In particular, the researchers were interested in understanding the steps in the formation of this iron cluster, starting from the initial seeding all the way to the development of an octa-nuclear iron cluster, a unique structure of eight iron cores.

Use of X-ray Structures

  • To do this, they used x-ray structures of human L-ferritin and horse spleen ferritin. These structures provide a detailed picture of the protein and allow for the observation of changes over time.
  • The researchers solved these structures at different time points after the proteins were exposed to a ferric salt, which is a compound of iron and another element or radical.
  • The x-ray structures revealed how the iron cluster begins as a single triiron(III) seed and over time, grows and develops into an extended iron core.

Role of Glutamate Residues

  • As per the study, glutamate residues played an essential role in this process. Glutamate is an amino acid that is present in proteins and plays a number of roles in the body, including the formation of protein structures and the synthesis of other amino acids.
  • The researchers found that these glutamate residues contribute coordination bonds and offer electrostatic guidance during the formation of the iron cluster. In other words, they help direct the placement of iron ions and hold them in place within the unfolding cluster.
  • This elucidates the mechanism behind how ferritin is able to store and eventually release iron within the body.

Conclusion

  • Findings from this research give us a more detailed understanding of the complex process of iron biomineralization in ferritin, and how it contributes to iron storage and release in living organisms.
  • This knowledge could be pivotal in developing treatments for health conditions related to iron imbalances, such as anemia and hemochromatosis, among others.

Cite This Article

APA
(2020). Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin. Chemistry, 26(26), 5770-5773. https://doi.org/10.1002/chem.202000064

Publication

Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
NlmUniqueID: 9513783
Country: Germany
Language: English
Volume: 26
Issue: 26
Pages: 5770-5773

Researcher Affiliations

MeSH Terms

  • Animals
  • Apoferritins / chemistry
  • Apoferritins / metabolism
  • Biological Phenomena
  • Ferritins / chemistry
  • Horses
  • Humans
  • Iron / chemistry

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Citations

This article has been cited 5 times.
  1. Jobichen C, Ying Chong T, Rattinam R, Basak S, Srinivasan M, Choong YK, Pandey KP, Ngoc TB, Shi J, Angayarkanni J, Sivaraman J. Bacterioferritin nanocage structures uncover the biomineralization process in ferritins.. PNAS Nexus 2023 Jul;2(7):pgad235.
    doi: 10.1093/pnasnexus/pgad235pubmed: 37529551google scholar: lookup
  2. Gehrer CM, Mitterstiller AM, Grubwieser P, Meyron-Holtz EG, Weiss G, Nairz M. Advances in Ferritin Physiology and Possible Implications in Bacterial Infection.. Int J Mol Sci 2023 Feb 28;24(5).
    doi: 10.3390/ijms24054659pubmed: 36902088google scholar: lookup
  3. Kuwata T, Sato D, Yanagida Y, Aoki E, Fujiwara K, Yoshimura H, Ikeguchi M. Morphological difference of Escherichia coli non-heme ferritin iron cores reconstituted in the presence and absence of inorganic phosphate.. J Biol Inorg Chem 2022 Sep;27(6):583-594.
    doi: 10.1007/s00775-022-01952-5pubmed: 35986810google scholar: lookup
  4. Bradley JM, Fair J, Hemmings AM, Le Brun NE. Key carboxylate residues for iron transit through the prokaryotic ferritin SynFtn.. Microbiology (Reading) 2021 Nov;167(11).
    doi: 10.1099/mic.0.001105pubmed: 34825885google scholar: lookup
  5. Davidov G, Abelya G, Zalk R, Izbicki B, Shaibi S, Spektor L, Shagidov D, Meyron-Holtz EG, Zarivach R, Frank GA. Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.. J Am Chem Soc 2020 Nov 18;142(46):19551-19557.
    doi: 10.1021/jacs.0c07565pubmed: 33166133google scholar: lookup
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