Iron Transport Mechanisms in Bacterial Systems
Summary
Bacteria require iron as a cofactor in essential processes such as respiration, DNA synthesis and defence against oxidative stress. Yet iron is scarce in many environments due to its low solubility and host-mediated sequestration. To overcome this, bacteria have evolved diverse uptake systems. Ferric iron (Fe3+) is commonly scavenged by siderophores, small high-affinity chelators secreted into the surroundings and recognised by specific outer-membrane receptors. Energy transduction across the membrane is often mediated by TonB-dependent transporters, which harness the proton motive force to import Fe3+–siderophore complexes. In Gram-positive bacteria and the periplasm of Gram-negatives, ABC transporters and periplasmic binding proteins shuttle iron to the cytoplasm. Under anaerobic or reducing conditions, ferrous iron (Fe2+) uptake predominates via the Feo system, a GTP-regulated membrane transporter. Regulation of these pathways is chiefly controlled by the ferric uptake regulator (Fur), which senses cytosolic iron and modulates gene expression. Together, these mechanisms enable bacteria to adapt to iron-limited niches, underpin virulence in pathogens and influence biogeochemical cycles.
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Iron Transport Mechanisms in Bacterial Systems publication trend
The graph below shows the total number of articles in iron transport mechanisms in bacterial systems across all publications each year (not limited to Nature Index journals).
Technical terms
Siderophore: A specialised small molecule secreted by bacteria to chelate and solubilise ferric iron for uptake.
TonB-dependent transporter: An outer-membrane protein that imports iron–siderophore complexes by coupling to the inner-membrane proton motive force via the TonB–ExbBD complex.
ABC transporter: A membrane-embedded ATP-binding cassette system that shuttles substrates, including iron-complexes, into the cytoplasm using ATP hydrolysis.
Feo system: A conserved ferrous iron (Fe2+) uptake pathway comprising the GTP-binding protein FeoB, its accessory protein FeoA and, in some species, FeoC.
Ferric uptake regulator (Fur): A metal-responsive transcription factor that represses or activates iron-related genes in response to cytosolic iron levels.
References
- Structural determinants of Vibrio cholerae FeoB nucleotide promiscuity. Journal of Biological Chemistry (2024).
- A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB. Journal of Biological Chemistry (2022).
- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system. BioMetals (2022).
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