Bacteria require efficient iron acquisition systems to infect and colonize the mammalian host. Neisseriaceae and Pasteurellaceae have developed an iron uptake system that involves iron removal from host glycoproteins. The human pathogen, Haemophilus influenzae, has a surface receptor complex containing transferrin binding proteins (TbpA and TbpB). This complex facilitates the release of iron from host transferrin and into the periplasm, where it binds to a periplasmic binding protein, ferric binding protein (FbpA). FbpA is part of the ABC transporter, FbpABC that transports iron from the periplasm into the cytoplasm. The interaction between FbpA and FbpBC is currently unknown. A series of site directed mutants were created to study this interaction based on models of other ABC transporters. We have developed a new novel reporter system to study this interaction. The results of this study have shown the lux reporter system to be more advantageous than past methods that evaluated iron uptake systems.