Corni Stefano
INFM Center on nanoStructures and bioSystems at Surfaces (S), Modena, Italy.
J Phys Chem B. 2005 Mar 3;109(8):3423-30. doi: 10.1021/jp0459920.
The total reorganization energy lambda of azurin is theoretically studied both for the electron self-exchange reaction and for the protein in the electrochemical scanning tunneling microscopy (ECSTM) setup. The results demonstrate the importance of the proximity between the active sites in the encounter complex to reduce lambda for the electron self-exchange reaction and quantifies the effects of the presence of an STM environment (tip and substrate) on lambda. A comparison of the calculated results with experimental data is performed, and the relative magnitudes of the inner and outer contributions to lambda are discussed.
本文从理论上研究了天青蛋白在电子自交换反应以及电化学扫描隧道显微镜（ECSTM）装置中的蛋白质体系下的总重组能λ。结果表明，在遭遇复合物中活性位点之间的接近程度对于降低电子自交换反应的λ至关重要，并量化了STM环境（探针和基底）的存在对λ的影响。将计算结果与实验数据进行了比较，并讨论了对λ的内、外贡献的相对大小。
