Institute of Biotechnology, University of Helsinki, P.O. Box 56, Helsinki 00014, Finland.
Institute of Biotechnology, University of Helsinki, P.O. Box 56, Helsinki 00014, Finland; Department of Physics, University of Helsinki, P.O. Box 64, Helsinki 00014, Finland.
Biochim Biophys Acta Bioenerg. 2018 Sep;1859(9):692-698. doi: 10.1016/j.bbabio.2018.03.009. Epub 2018 Mar 19.
Cytochrome c oxidase is a remarkable energy transducer that seems to work almost purely by Coulombic principles without the need for significant protein conformational changes. In recent years it has become possible to follow key partial reactions of the catalytic cycle in real time, both with respect to electron and proton movements. These experiments have largely set the stage for the proton pump mechanism. The structures of the catalytic binuclear heme‑copper site that is common to the huge family of heme‑copper oxidases, are today well understood throughout the catalytic cycle of oxygen reduction to water based on both spectroscopic studies and quantum chemical calculations. Here, we briefly review this progress, and add some recent details into how the proton pump mechanism is protected from failure by leakage.
细胞色素 c 氧化酶是一种卓越的能量转换器，它似乎几乎完全通过库仑原理工作，而不需要显著的蛋白质构象变化。近年来，人们已经能够实时跟踪催化循环中的关键部分反应，无论是电子还是质子的运动。这些实验在很大程度上为质子泵机制奠定了基础。对于巨大的血红素铜氧化酶家族所共有的催化双核血红素-铜位点的结构，基于光谱研究和量子化学计算，在氧还原为水的整个催化循环中，现在已经得到了很好的理解。在这里，我们简要回顾一下这方面的进展，并添加一些最近的细节，说明质子泵机制如何通过防止泄漏来防止失效。
