Inhibitor-enhanced electron transfer: copper cytochrome c as a redox-inert probe of ternary complexes.
Inhibitor-enhanced electron transfer: copper cytochrome c as a redox-inert probe of ternary complexes.
复制标题
抑制剂增强电子转移:铜细胞色素 c 作为三元复合物的氧化还原惰性探针。
DOI:
10.1126/science.7618081
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发表时间:
1995
期刊:
影响因子:
--
通讯作者:
Hoffman,BM
中科院分区:
文献类型:
--
作者:
Zhou,JS;Nocek,JM;DeVan,ML;Hoffman,BM
Copper-substituted cytochrome c (CuCc) has been used as a structurally faithful, redoxinert inhibitor to probe the mechanism of electron transfer (ET) between Cc molecules and cytochrome c peroxidase (CcP). This inhibitor enhances photoinduced ET quenching of the triplet excited state of a zinc-substituted protein (ZnCcP or ZnCc) by its iron(III) partner (Fe3+Cc or Fe3+CcP). These results show that CcP and Cc form a ternary complex in which one Cc molecule binds tightly at a surface domain of CcP having low ET reactivity, whereas the second Cc molecule binds weakly to the 1:1 complex at a second domain with markedly greater (∼103) reactivity. These results also rule out the possibility that Cc bound at the second domain cooperatively enhances ET to Cc at the first domain. The multiphasic kinetics observed for the photoproduced ET intermediate do not reflect electron self-exchange between two Cc molecules within the ternary complex.