分析古细菌A1AO-ATP合酶的单个FRET标记的A1部分的构象变化
Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
摘要：
ATP酶利用质子动力合成ATP。相反，这些膜包埋的酶也可以水解ATP，将质子泵送过膜。为了防止浪费的ATP水解，在细菌、古细菌、叶绿体和线粒体中存在对ATP酶的不同控制机制。单分子Förster共振能量转移（smFRET）表明，大肠杆菌酶中旋转亚基β的C-末端改变其构象以阻止ATP水解。在此之前，我们研究了古菌Methanosarcina mazei Gö 1的A1 AO-ATP合酶亚基F的相关构象变化。在这里，我们分析了荧光供体和受体染料的寿命，以区分构象变化和潜在的文物smFRET信号。
英文摘要：
ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit epsilon in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously we investigated the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyze the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals for conformational changes and potential artefacts.
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