PROTEIN ELECTRON-TRANSFER RATES SET BY THE BRIDGING SECONDARY AND TERTIARY STRUCTURE
PROTEIN ELECTRON-TRANSFER RATES SET BY THE BRIDGING SECONDARY AND TERTIARY STRUCTURE
复制标题
DOI：
10.1126/science.1656523
复制
发表时间：
1991-05-31
期刊：
影响因子：
56.9
通讯作者：
ONUCHIC, JN
中科院分区：
文献类型：
--
作者：
BERATAN, DN;BETTS, JN;ONUCHIC, JN
蛋白质中远距离电子转移的速率随着距离的增加而迅速降低，这表明存在电子隧穿过程。计算预测，天然蛋白质中电子转移的距离依赖是由蛋白质的结构基序控制的。蛋白质的螺旋和薄片含量以及这些二级结构单元的三级排列决定了该蛋白质中电子偶联的距离依赖性。计算使用了一个隧道通路模型，该模型以前曾成功应用于粗糙化蛋白质。该分析对电子转移蛋白中电子耦合的平均距离衰减常数进行了排序，并确定了与电荷定位位点耦合的氨基酸比其平均距离更强或更弱。
The rate of long-distance electron transfer in proteins rapidly decreases with distance, which is indicative of an electron tunneling process. Calculations predict that the distance dependence of electron transfer in native proteins is controlled by the protein's structural motif. The helix and sheet content of a protein and the tertiary arrangement of these secondary structural units define the distance dependence of electronic coupling in that protein. The calculations use a tunneling pathway model applied previously with success to ruthenated proteins. The analysis ranks the average distance decay constant for electronic coupling in electron transfer proteins and identifies the amino acids that are coupled to the charge localization site more strongly or weakly than average for their distance.