Please use this identifier to cite or link to this item:
Title: X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: The coordination properties of the copper ion
Authors: L., Banci
I., Bertini
R. D., Conte
Mangani, Stefano 
W., Meyer Klaucke
Keywords: XAS; copper transport; metallochaperone; CopZ
Issue Date: 2003
Project: None 
XAS studies have been performed, under various experimental conditions, on a copper(I)transporting protein, CopZ, of Bacillus subtilis. The copper(I) ion, reduced with dithiothreitol, is three-coordinate with three sulfur donor atoms, two of which presumably provided by the protein and one by dithiothreitol. If a molar excess of acetate (15 mM; 5:1 respect to CopZ) or citrate (6 mM; 2:1 respect to CopZ) is present in solution, the EXAFS spectra suggest the presence of a dimeric form involving a close contact between Cu(I) ions from two molecules, where Cu is still three-coordinate. H-1 and N-15 NMR data provide further structural details. If copper reduction is accomplished with ascorbate, the data indicate that one oxygen of ascorbate enters in the first-coordination sphere of copper, together with two sulfur atoms, in a dimeric form of the protein. These results are instructive and have been discussed with respect to the molecular basis of copper trafficking.
ISSN: 0006-2960
DOI: 10.1021/bi0205810
Appears in Collections:Publications

Show full item record

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.