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

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...

Full description

Saved in:
Bibliographic Details
Published in:Inorganic chemistry 2007-05, Vol.46 (11), p.4560-4568
Main Authors: Djoko, Karrera Y, Xiao, Zhiguang, Huffman, David L, Wedd, Anthony G
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Conserved Sequence
Copper - metabolism
Escherichia coli - chemistry
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Molecular Sequence Data
Oxidation-Reduction
Protein Structure, Tertiary
Pseudomonas syringae - chemistry
Pseudomonas syringae - metabolism
Sequence Alignment
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0020-1669
1520-510X
DOI:10.1021/ic070107o