Characterization of heme transport proteins from pathogenic bacteria

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Iron is involved in a wide range of essential functions in various metabolic pathways ; therefore, most bacteria have some form of iron-scavenging system in order to survive. Heme acquisition system A(HasA), secreted by various gram-negative pathogens, uses a unique histidine-iron-tyrosine(His-Fe-Tyr) or an iron-tyrosine(Fe-Tyr) coordination to scavenge heme. Our results suggest that the binding of heme in apoprotein is initiated by interactions between heme and hydrophobic residues in the heme binding pocket. Subsequent coordination of Tyr to the heme iron complete holoprotein formation.