铜结合与转运的保守机制。大肠杆菌的铜抗性蛋白PcoC与丁香假单胞菌的CopC的比较。
Conserved mechanism of copper binding and transfer. A comparison of the copper-resistance proteins PcoC from Escherichia coli and CopC from Pseudomonas syringae.
作者信息
Djoko Karrera Y, Xiao Zhiguang, Huffman David L, Wedd Anthony G
机构信息
School of Chemistry, University of Melbourne, Parkville, Victoria 3052, Australia.
出版信息
Inorg Chem. 2007 May 28;46(11):4560-8. doi: 10.1021/ic070107o. Epub 2007 May 4.
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.
来自大肠杆菌的铜抗性蛋白PcoC和来自丁香假单胞菌的CopC具有67%的序列同一性，但报道的PcoC的化学性质（Peariso, K.; Huffman, D. L.; Penner-Hahn, J. E.; O'Halloran, T. V. J. Am. Chem. Soc. 2003, 125, 342 - 343）与CopC的化学性质（Zhang, L.; Koay, M.; Maher, M. J.; Xiao, Z.; Wedd, A. G. J. Am. Chem. Soc. 2006, 128, 5834 - 5850）明显不同。已确定不一致的来源，并且His1被确认为每种蛋白质中前所未有的双齿配体。获得真正的野生型PcoC蛋白使得能够明确观察到分子间氧化还原铜转移反应中涉及的中间体。
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