Studies on interprotein electron transfer using artificial protein complexes

通常，氧化还原伴侣蛋白在蛋白质间电子转移反应期间形成瞬时复合物。目前已经知道，由于复合物结构的构象变化，ET有效转运蛋白存在一些调节机制。然而，调制的大部分细节仍然未知，因为由于不稳定性，很难确定复杂的结构。因此，我们计划对人工构建的复合物和天然融合蛋白的结构和生物物理性质进行分析。基于他们的数据，我们讨论并提出了前所未有的蛋白质间ET反应的机制。

Generally, the redox-partner proteins form a transient complex during the inter-protein electron transfer reaction. It has been known that there are some modulation mechanisms for effective interportein ET due to the conformational changes in the complex structure. However, most of the details for modulation remain unknown, because it is quite difficult to determine the complex structure due to the instability. So, we planed to analyze the structures and biophysical properties for the complexes constructed artificially and the naturally fused proteins. Based on their data, we discuss and propose the unprecedented mechanism for interprotein ET reaction.