On the role of strain in blue copper proteins
On the role of strain in blue copper proteins
复制标题
菌株在蓝铜蛋白中的作用
DOI：
10.1007/s007750000147
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
K. Pierloot
中科院分区：
文献类型：
--
作者：
U. Ryde;M. Olsson;B. Roos;Jan O.A. De Kerpel;K. Pierloot
摘要。对蓝铜蛋白的结构和功能进行了理论研究。我们研究了氧化和还原铜位的最佳真空几何形状、三角形和四边形Cu（II）结构的相对稳定性、结构与电子能谱、重组能和还原势之间的关系。我们的计算没有支持菌株在这些蛋白质的功能中起重要作用的建议；相反，我们的结果表明，蛋白质中遇到的结构接近其最佳真空几何形状（在7 kJ/mol以内）。我们强调定义应变的意义和量化应变能或力的重要性，以便使应变假设可检验。
Abstract. Theoretical investigations of the structure and function of the blue copper proteins are described. We have studied the optimum vacuum geometry of oxidised and reduced copper sites, the relative stability of trigonal and tetragonal Cu(II) structures, the relation between the structure and electronic spectra, the reorganisation energy, and reduction potentials. Our calculations give no support to the suggestion that strain plays a significant role in the function of these proteins; on the contrary, our results show that the structures encountered in the proteins are close to their optimal vacuum geometries (within 7 kJ/mol). We stress the importance of defining what is meant by strain and of quantifying strain energies or forces in order to make strain hypotheses testable.