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Copper Binding To Riboflavin Binding Protein‐ The Role Of Phosphoserine Residues
Author(s) -
Brandt Eric,
Smith Sheila R,
Benore Marilee
Publication year - 2009
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.23.1_supplement.894.6
Subject(s) - phosphoserine , copper , chemistry , histidine , biochemistry , binding site , binding protein , copper protein , imidazole , serine , amino acid , phosphorylation , organic chemistry , gene
Riboflavin Binding Protein (RBP) is a hen glyco‐phospho‐protein that transports the nutrient riboflavin to the oviduct and oocyte. Recent work in our labs indicates the protein also binds copper in a 1:1 ratio in vitro. The site of copper binding to Riboflavin Binding Protein is unclear, although it appears Histidine residues are involved. We are interested in determining if the phosphoserine residues participate in copper binding. It is possible, though unlikely, that the metal binds to one of the numerous phosphoserine residues or that the phosphoserine residues alter the binding affinity or ratio. RBP was dephosphorylated, dialyzed against copper, and the copper binding characterized using Atomic Absorption Spectroscopy. Evidence suggests that the dephosphorylated protein can still bind copper. This work is supported by a grant from the University of MI at Dearborn.