MAPPING ELECTRON-TUNNELING PATHWAYS - AN ALGORITHM THAT FINDS THE MINIMUM LENGTH MAXIMUM COUPLING PATHWAY BETWEEN ELECTRON-DONORS AND ACCEPTORS IN PROTEINS
MAPPING ELECTRON-TUNNELING PATHWAYS - AN ALGORITHM THAT FINDS THE MINIMUM LENGTH MAXIMUM COUPLING PATHWAY BETWEEN ELECTRON-DONORS AND ACCEPTORS IN PROTEINS
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DOI：
10.1021/ja00037a004
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发表时间：
1992-05-20
影响因子：
15
通讯作者：
ONUCHIC, JN
中科院分区：
文献类型：
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作者：
BETTS, JN;BERATAN, DN;ONUCHIC, JN
蛋白质的共价连接、氢键连接和货车范德华连接可以用称为图的几何对象来表示。在这些图中，顶点代表键，它们之间的连接，边，代表键-键相互作用。我们描述了一个模型，在该模型中，边的长度与相互作用的键对之间的波函数衰减，和一个最小距离图搜索算法被用来找到这些分子中占主导地位的电子供体-受体相互作用的途径。相对电子转移速率的预测可以从这些路径长度。结果与许多实验测得的电子转移率是一致的，虽然存在一些异常。将供体（或受体）与给定蛋白质中的每一个其他原子之间的途径偶联呈现为颜色编码图，为定制的电子转移蛋白质提供了设计工具。
The covalent, hydrogen bonded, and van der Waals connectivity of proteins can be represented with geometrical objects called graphs. In these graphs, vertices represent bonds and the connections between them, edges, represent bond-bond interactions. We describe a model in which edge lengths are associated with the wave function decay between interacting pairs of bonds, and a minimum distance graph-search algorithm is used to find the pathways that dominate electron donor-acceptor interactions in these molecules. Predictions of relative electron transfer rates can be made from these pathway lengths. The results are consistent with many experimentally measured electron-transfer rates, although some anomalies exist. Presentation of the pathway coupling between the donor (or acceptor) and every other atom in a given protein as a color-coded map provides a design tool for tailored electron-transfer proteins.