Riboflavin Binding Protein (RBP) is an essential vitamin carrier found in all oviparous species.  RBP piggybacks into the embryo via a phosvitin specific receptor, and is actively transported into the embryo before laying, even in the absence of bound riboflavin.  Recent work in our labs has shown that RBP will bind copper in vitro under dialysis conditions.  The copper is bound 1:1 in a Type II copper binding site with a single histidine and 3-4 unknown N/O type ligands.  The copper is partially reduced, though dialysis is carried out against cupric salts in aerobic conditions.  Based on spectroscopic (XAS, EPR), electrochemical, and thermodynamic (ITC) studies, we hypothesize a role for RBP in copper transport and storage in avian embryonic development.  The egg is a unique model for metal transport and storage since all necessary nutrients must be delivered to the embryo before laying, and stored, potentially for long periods under harsh conditions. Sequence comparison to RBPs from 18 other oviparous species suggests that this role may be conserved across all egg-layers.

Smuggled cargo: copper binding to riboflavin binding protein

2019 Spring National Meeting

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