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Updated: Mar 13, 2026
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Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
Published on: December 13, 2016
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Electrostatic and Structural Bases of Fe2+ Translocation through Ferritin Channels
Balasubramanian Chandramouli1,2, Caterina Bernacchioni3, Danilo Di Maio4,2
1From the Scuola Normale Superiore, Piazza dei Cavalieri 7, I-56126 Pisa, bala.chandramouli@sns.it.
The Journal of Biological Chemistry
|October 21, 2016
Summary
This study reveals how iron ions (Fe2+) move through ferritin protein channels. Findings clarify the iron transport mechanism via the C3 channel in vertebrate ferritins, aiding future biomedical applications.
Area of Science:
- Biochemistry
- Structural Biology
- Biophysics
Background:
- Ferritin is a 24-mer protein cage storing iron (>2000 atoms).
- Ferritin channels (C3 and C4 axes) mediate iron transport.
- Ferritin's potential for drug delivery and imaging is recognized.
Purpose of the Study:
- To elucidate the Fe2+ transport mechanism through ferritin channels.
- To characterize Fe2+ translocation in wild-type and mutant bullfrog ferritin (Rana catesbeiana H').
Main Methods:
- Extensive molecular dynamics simulations.
- Site-directed mutagenesis.
- Kinetic measurements.
Main Results:
- Detailed structural features governing Fe2+ translocation were identified.
- The C3 channel was confirmed as the sole iron-permeable pathway in vertebrate ferritins.
- A putative mechanism for Fe2+ transport through the C3 channel was proposed.
Conclusions:
- Understanding Fe2+ permeation through ferritin channels is crucial.
- Findings provide insights for engineering ferritin channels for biomedical applications.
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