Riboflavin Binding Protein (RBP) has been observed in vitro to bind copper in a 1:1 molar ratio in vitro.  Determination of the binding constant of this protein for copper is complicated by the simultaneous reduction of a significant portion of the copper upon binding. Ongoing efforts in our lab to deconvolute the binding event using a combination of electrochemical and physical measurements will be presented.  We compare the interaction with copper by apo- and holo- RBP (riboflavin free or bound) in the presence and absence of oxidizing agents and in the presence or absense of oxygen.   As part of this work, we have begun to explore the role of the RBP as a possible vehicle for delivery of copper to the mineral storage protein phosvitin.  We will present data obtained from cylcic voltammetry, isothermal titration calorimetry, and surface plasmon resonance.

Thermodynamic studies on the interaction between riboflavin binding protein and phosvitin in the presence and absence of copper

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.