Riboflavin binding protein contains a type II copper binding site.
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.
Smith
Sheila R
SR
Department of Natural Sciences, University of Michigan - Dearborn, 4901 Evergreen Road, Dearborn, MI 48128, United States. sheilars@umd.umich.edu <sheilars@umd.umich.edu>
Pala
Irina
I
Benore-Parsons
Marilee
M
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D003300:Copper