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Updated: Jul 20, 2026

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Riboflavin binding protein contains a type II copper binding site
Sheila R Smith1, Irina Pala, Marilee Benore-Parsons
1Department of Natural Sciences, University of Michigan - Dearborn, 4901 Evergreen Road, Dearborn, MI 48128, United States. sheilars@umd.umich.edu <sheilars@umd.umich.edu>
Abstract:
Riboflavin binding protein, purified from egg white, binds copper(II) under dialysis conditions in an approximately 1:1 molar ratio. Results further indicate a small, but not negligible, amount of copper is present in the protein as purified from egg white. Electron paramagnetic resonance indicates a single type II copper site present in the protein. These results suggest the possibility of a previously unknown function of riboflavin binding protein in the storage or transport of copper.
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