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Enterobactin: An archetype for microbial iron transport
TLDR
Study of the chemistry, regulation, synthesis, recognition, and transport of enterobactin make it perhaps the best understood of the siderophore-mediated iron uptake systems, displaying a lot of function packed into this small molecule.
Iron Traffics in Circulation Bound to a Siderocalin (Ngal)-Catechol Complex
TLDR
Using chemical screens, crystallography, and fluorescence methods, it is reported that Scn-Ngal binds iron together with a small metabolic product called catechol, which represents an unforeseen microbial-host interaction, which mimics Scsiderophore interactions, but instead traffics iron in aseptic tissues.
The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2
TLDR
This work shows that the iroA gene cluster, found in many pathogenic strains of Gram-negative enteric bacteria, including E. coli, Salmonella spp.
Anthrax pathogen evades the mammalian immune system through stealth siderophore production
TLDR
The results indicate that the blockade of bacterial siderophore-mediated iron acquisition by siderocalin is not restricted to enteric pathogenic organisms and may be a general defense mechanism against several different bacterial species.
Microbial iron transport via a siderophore shuttle: a membrane ion transport paradigm.
TLDR
It is shown that the siderophore and Fe(3+) enter the bacterium together, a ligand exchange step occurs in the course of the transport, and a redox process is not involved in iron exchange.
Petrobactin-mediated iron transport in pathogenic bacteria: coordination chemistry of an unusual 3,4-catecholate/citrate siderophore.
TLDR
Solution thermodynamic and kinetic measurements show that incorporation of 3,4-catecholate subunits into the siderophore structure does not enhance its affinity for iron as compared to hydroxamate units, but it promotes fast iron removal from human diferric transferrin.
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