What are the structural features of the active site that define binuclear copper proteins function?

被引:3
|
作者
Bubacco, L [1 ]
van Gastel, M
Benfatto, M
Tepper, AWJW
Canters, GW
机构
[1] Univ Padua, Dipartimento Biol, Padua, Italy
[2] Leiden Univ, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands
[3] Ist Nazl Fis Nucl, Lab Nazl Frascati, I-00044 Frascati, Italy
关键词
binuclear; copper; tyrosinase; hemocyanin; active site;
D O I
10.1016/j.micron.2003.10.046
中图分类号
TH742 [显微镜];
学科分类号
摘要
The structural basis that define the physiological functions of binuclear copper enzymes is discussed in the frame of the data generated by a broad spectroscopic approach, spanning from paramagnetic NMR and pulsed EPR to x-ray absorption spectroscopies. The structural features discussed for the different oxidation and ligation states accessible to a binuclear copper sites are the coordination geometry for the first and second shell, the metal-metal distance and the role of the bridging exogenous ligand(s). A structural model will be presented to rationalize both the differentiation in function within the protein families and the reaction mechanism of those proteins that are enzymatically active. (C) 2003 Elsevier Ltd. All rights reserved.
引用
收藏
页码:143 / 145
页数:3
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