Investigation of the Copper Binding Site and the Role of Histidine as a Ligand in Riboflavin Binding Protein
Citations Over Time
Abstract
Riboflavin Binding Protein (RBP) binds copper in a 1:1 molar ratio, forming a distinct well-ordered type II site. The nature of this site has been examined using X-ray absorption and pulsed electron paramagnetic resonance (EPR) spectroscopies, revealing a four coordinate oxygen/nitrogen rich environment. On the basis of analysis of the Cambridge Structural Database, the average protein bound copper-ligand bond length of 1.96 A, obtained by extended x-ray absorption fine structure (EXAFS), is consistent with four coordinate Cu(I) and Cu(II) models that utilize mixed oxygen and nitrogen ligand distributions. These data suggest a Cu-O 3N coordination state for copper bound to RBP. While pulsed EPR studies including hyperfine sublevel correlation spectroscopy and electron nuclear double resonance show clear spectroscopic evidence for a histidine bound to the copper, inclusion of a histidine in the EXAFS simulation did not lead to any significant improvement in the fit.
Related Papers
- → EPR and ENDOR Studies of Shallow Donors in SiC(2010)16 cited
- → CW EPR and DEER Methods to Determine BCL-2 Family Protein Structure and Interactions: Application of Site-Directed Spin Labeling to BAK Apoptotic Pores(2018)4 cited
- → Fourier-Transform EPR(2017)6 cited
- → Electron Paramagnetic Resonance Spectroscopy of Inorganic Materials(2013)1 cited
- → Electron Paramagnetic Resonance Spectroscopy(2017)