title: Conserved mechanism of copper binding and transfer. A comparison of the copper-resistance proteins PcoC from Escherichia coli and CopC from Pseudomonas syringae.
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.
authors.affiliation: School of Chemistry, University of Melbourne, Parkville, Victoria 3052, Australia.
authors.forename: Karrera Y
authors.initials: KY
authors.lastname: Djoko
authors.forename: Zhiguang
authors.initials: Z
authors.lastname: Xiao
authors.forename: David L
authors.initials: DL
authors.lastname: Huffman
authors.forename: Anthony G
authors.initials: AG
authors.lastname: Wedd
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence; D003300:Copper / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D017434:Protein Structure, Tertiary; D044224:Pseudomonas syringae / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; C071265:CopC protein, Bacteria; D029968:Escherichia coli Proteins; C462541:PcoC protein, E coli; D003300:Copper