Curry W B, Grabe M D, Kurnikov I V, Skourtis S S, Beratan D N, Regan J J, Aquino A J, Beroza P, Onuchic J N
Department of Chemistry, University of Pittsburgh, Pennsylvania 15260, USA.
J Bioenerg Biomembr. 1995 Jun;27(3):285-93. doi: 10.1007/BF02110098.
The simplest views of long-range electron transfer utilize flat one-dimensional barrier tunneling models, neglecting structural details of the protein medium. The pathway model of protein electron transfer reintroduces structure by distinguishing between covalent bonds, hydrogen bonds, and van der Waals contacts. These three kinds of interactions in a tunneling pathway each have distinctive decay factors associated with them. The distribution and arrangement of these bonded and nonbonded contacts in a folded protein varies tremendously between structures, adding a richness to the tunneling problem that is absent in simpler views. We review the pathway model and the predictions that it makes for protein electron transfer rates in small proteins, docked proteins, and the photosynthetic reactions center. We also review the formulation of the protein electron transfer problem as an effective two-level system. New multi-pathway approaches and improved electronic Hamiltonians are described briefly as well.
远程电子转移最简单的观点采用平面一维势垒隧穿模型，忽略了蛋白质介质的结构细节。蛋白质电子转移的途径模型通过区分共价键、氢键和范德华接触重新引入了结构。隧穿途径中的这三种相互作用各自都有与之相关的独特衰减因子。在折叠蛋白质中，这些键合和非键合接触的分布和排列在不同结构之间差异极大，给隧穿问题增添了简单观点中所没有的丰富性。我们回顾了途径模型及其对小蛋白质、对接蛋白质和光合反应中心中蛋白质电子转移速率的预测。我们还回顾了将蛋白质电子转移问题表述为有效两能级系统的情况。同时简要描述了新的多途径方法和改进的电子哈密顿量。
