Chemistry, 2013

    Analysis of the Binding of Metal Ions to Riboflavin Binding Protein
    Morgan Hall, Marissa Snyder
    Mentor: Tracey Arnold Murray

    Riboflavin binding protein (RBP) is a protein used primarily for the transport and storage of riboflavin, also known as Vitamin B2, in avian and reptilian eggs. Recent studies have shown the binding of copper (II) to RBP in a 1:1 molar ratio after dialyzing the RBP with copper, suggesting that riboflavin transport and storage may not be RBP’s only function. Dialysis of RBP against additional metals at both a 1:1 molar ratio and physiological ratios was used to test the binding of other metal cations to RBP. The RBP concentration of the resulting samples was determined using UV-Vis spectrophotometry and the bound metal ion concentration was determined using atomic absorbance spectroscopy. Results confirm the binding of other metals to RBP, and several of these metals are shown to outcompete copper (II) for RBP binding. These results also suggest that RBP may have another function, such as the transport, storage, and controlled release of essential metals inside the egg.