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Iron core mineralisation in prokaryotic ferritins
Nick E Le Brun1, Allister Crow, Michael E P Murphy
1Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK. n.le-brun@uea.ac.uk
Biochimica Et Biophysica Acta
|April 15, 2010
Summary
Prokaryotic ferritins, including bacterioferritins (BFRs) and bacterial ferritins (Ftns), manage iron storage and toxicity. Recent studies reveal at least two distinct iron mineralization mechanisms, influenced by structural variations in their catalytic centers.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- Prokaryotes utilize bacterioferritins (BFRs) and bacterial ferritins (Ftns) to manage iron uptake, storage, and detoxification.
- These proteins sequester iron as a safe, bio-available mineral, crucial for cellular iron homeostasis.
- Homologues of bacterial ferritins (Ftns) are increasingly identified in archaeal species.
Purpose of the Study:
- To review current understanding of iron mineralization mechanisms in prokaryotic ferritins.
- To highlight recent structural, spectroscopic, and kinetic studies on these iron-binding proteins.
- To elucidate the diverse strategies employed by prokaryotic ferritins for iron management.
Main Methods:
- Review of existing literature on prokaryotic ferritins.
- Emphasis on structural, spectroscopic, and kinetic analyses.
- Comparative analysis of different ferritin sub-families (BFRs and Ftns).
Main Results:
- Prokaryotic ferritins employ at least two distinct mechanisms for iron mineralization.
- The ferroxidase center plays a key role, acting either as a catalytic site for Fe(2+) oxidation or a gated pore for Fe(3+) transfer.
- Structural differences, particularly around the catalytic center, underpin these mechanistic variations.
Conclusions:
- Prokaryotic ferritins exhibit diverse iron core mineralization pathways.
- Structural variations at the catalytic center are primary drivers of mechanistic differences.
- Subtle structural nuances also significantly influence the iron chemistry within these proteins.
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