Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.
Curr Opin Struct Biol. 2011 Aug;21(4):532-40. doi: 10.1016/j.sbi.2011.07.002. Epub 2011 Aug 8.
Complex I is the first enzyme of the respiratory chain and plays a central role in cellular energy production. It has been implicated in many human neurodegenerative diseases, as well as in ageing. One of the biggest membrane protein complexes, it is an L-shaped assembly consisting of hydrophilic and membrane domains. Previously, we have determined structures of the hydrophilic domain in several redox states. Last year was marked by fascinating breakthroughs in the understanding of the complete structure. We described the architecture of the membrane domain and of the entire bacterial complex I. X-ray analysis of the larger mitochondrial enzyme has also been published. The core subunits of the bacterial and mitochondrial enzymes have remarkably similar structures. The proposed mechanism of coupling between electron transfer and proton translocation involves long-range conformational changes, coordinated in part by a long α-helix, akin to the coupling rod of a steam engine.
复合体 I 是呼吸链的第一酶，在细胞能量产生中起着核心作用。它与许多人类神经退行性疾病以及衰老有关。作为最大的膜蛋白复合物之一，它是由亲水和膜结构域组成的 L 形组装体。此前，我们已经确定了几种氧化还原状态下的亲水结构域结构。去年在全面了解完整结构方面取得了令人瞩目的突破。我们描述了膜结构域和整个细菌复合体 I 的结构。更大的线粒体酶的 X 射线分析也已发表。细菌和线粒体酶的核心亚基具有惊人相似的结构。提出的电子传递与质子转移偶联机制涉及长程构象变化，部分由长α-螺旋协调，类似于蒸汽机的连杆。
