Association of Copper to Riboflavin Binding Protein; Characterization by EPR and XAS

Journal Article · Tue Jan 01 04:00:00 EST 2008 · The Open Inorganic Chemistry Journal

OSTI ID:960191

Smith, S; Bencze, K; Wasiukanis, K; Stemmler, T; Benore-Parsons, M

The association of copper to Riboflavin Binding Protein (RBP) from egg white has been studied by electron paramagnetic resonance (EPR) and X-ray absorption (XAS) spectroscopies. The type II site contains a mix of copper I and II in an oxygen rich environment. The association of copper to Riboflavin Binding Protein (RBP) from egg white has been studied by electron paramagnetic resonance (EPR) and X-ray absorption (XAS) spectroscopies in order to provide insight into how this essential protein may transport and store copper in avian embryos. Riboflavin Binding Protein, RBP, purified from avian egg white, has been shown to bind copper in a 1:1 molar ratio when dialyzed against copper(II) [1]. While the egg is a unique environment and quite rich in copper, the mechanisms by which this copper is delivered during development and stored for eventual use remain unclear [2]. Since RBP is already identified in the active transport of the cofactor riboflavin to the egg, evidence of its copper binding ability may suggest an additional role for RBP in the transport and storage of copper.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 960191
• Report Number(s): BNL--83177-2009-JA
• Journal Information: The Open Inorganic Chemistry Journal, Journal Name: The Open Inorganic Chemistry Journal Vol. 2
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
ABSORPTION SPECTROSCOPY
COPPER
ELECTRON SPIN RESONANCE
EMBRYOS
OXYGEN
PROTEINS
RIBOFLAVIN
STORAGE
TRANSPORT
X-RAY SPECTROSCOPY
national synchrotron light source