Conserved mechanism of copper binding and transfer.: A comparison of the copper-resistance proteins PcoC from Escherichia coli and CopC from Pseudomonas syringae

被引：55

作者：

Djoko, Karrera Y.

Xiao, Zhiguang ^{[1
]}

Huffman, David L.

Wedd, Anthony G.

机构：

[1] Univ Melbourne, Sch Chem, Parkville, Vic 3052, Australia

[2] Bio21 Mol Sci & Biotechnol Inst, Parkville, Vic 3010, Australia

[3] Western Michigan Univ, Dept Chem, Kalamazoo, MI 49008 USA

来源：

INORGANIC CHEMISTRY | 2007年 / 46卷 / 11期

关键词：

D O I：

10.1021/ic070107o

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

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.

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页码：4560 / 4568

页数：9

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