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Exploring a Possible Role in Copper Transport and Storage for the Vitamin Carrier, Riboflavin Binding Protein
Author(s) -
Smith Sheila,
Benore Marilee
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.912.15
Subject(s) - copper , copper protein , phosvitin , chemistry , histidine , electron paramagnetic resonance , plastocyanin , binding protein , binding site , transport protein , crystallography , biochemistry , organic chemistry , amino acid , enzyme , protein kinase a , physics , photosystem i , nuclear magnetic resonance , chloroplast , gene
Riboflavin Binding Protein (RBP) has been shown previously to bind copper in vitro in a one to one molar ratio. The binding site, characterized by EPR, EXAFS, ESEEM and ENDOR spectropcopies is a well ordered Type II copper site with one histidine ligand and 2–3 oxygenic ligands. Copper‐loaded RBP was dialyzed with the egg protein phosvitin, previously shown to bind multiple equivalents of copper. The proteins were separated by FPLC and the copper content was measured by graphite furnace AA spectroscopy. All of the copper was transferred to the phosvitin. Relative binding constants of the two proteins were determined. We present a hypothesis for the role of copper binding and protein‐protein interaction in copper transport into the avian egg.