Conserved Mechanism of Copper Binding and Transfer. A Comparison of the Copper-Resistance Proteins PcoC from <i>Escherichia coli</i> and CopC from <i>Pseudomonas syringae</i>

Abstract

The copper-resistance proteins PcoC from Escherichia coli and CopC from Pseudomonas syringae exhibit 67% sequence identity, but the chemistry reported for PcoC (Peariso, K.; Huffman, D. L.; Penner-Hahn, J. E.; O'Halloran, T. V. J. Am. Chem. Soc. 2003, 125, 342-343) was distinctly different from that reported for CopC (Zhang, L.; Koay, M.; Maher, M. J.; Xiao, Z.; Wedd, A. G. J. Am. Chem. Soc. 2006, 128, 5834-5850). The source of the inconsistency has been identified, and His1 is confirmed as an unprecedented bidentate ligand in each protein. Access to a bona fide wild-type PcoC protein allowed unequivocal observation of intermediates involved in intermolecular redox copper transfer reactions.