Riboflavin binding protein (RBP) is an appealing subject of study because it is actively transported into avian embryos, even in the absence of its only known substrate, riboflavin. Since nature does not often waste energy on purposeless proteins, another role as a Cu transporter is hypothesized. Previous studies have shown that RBP binds Cu in a 1:1 molar ratio at a type II binding site.  Still, the question arises as to whether this binding is functional or adventitious.  In an effort to answer this question, we are currently exploring two approaches.  One of the goals in our group is the determination of the CuRBP binding constant.  The failure of several traditional methods for this determination have led us to develop a novel technique.  Furthermore, we are looking at other divalent metal ions, in particular zinc, to determine if the binding of copper is specific. In the event of Zn binding, competition analyses with Cu will be conducted, as will the determination of the ZnRBP binding constant.

Exploring an alternate role for Riboflavin Binding Protein in copper transport and storage

243rd National Meeting (2012)

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