Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
Date of Issue2018
Single Molecule Spectroscopy and Superresolution Imaging XI
School of Biological Sciences
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 ε in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.
Progress in Biomedical Optics and Imaging - Proceedings of SPIE
© 2018 Society of Photo-optical Instrumentation Engineers (SPIE). This paper was published in Progress in Biomedical Optics and Imaging - Proceedings of SPIE and is made available with permission of Society of Photo-optical Instrumentation Engineers (SPIE). The published version is available at: [http://dx.doi.org/10.1117/12.2286785]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.