Riboflavin binding protein (RBP) is an essential vitamin (B<sub>2</sub>) carrier found in all oviparous species. RBP is purified from either the egg yolk or white without copper bound, but binds copper in a 1:1 molar ratio upon dialysis against cupric salts under aerobic conditions. Spectroscopic data (XAS, EPR) support a Type II site with a single histidine ligand, and 3-4 unknown N/O ligands. The reducing agent and reduction potential have not been previously identified. Cyclic voltammetry on copper bound-RBP was performed using a gold electrode modified with aldrithiol-4 to determine the redox activity and the reduction potential of both apo- and holo- (Rf-/+)- RBP loaded with copper.

Determination of the reduction potential of copper bound- riboflavin binding protein

2019 Spring National Meeting

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