2018/01/15 by Hendrik Sielaff, Dhirendra Singh, Sielaff, Hendrik +6
Biochemistry, Genetics and Molecular Biology · Chemistry · #ATP Synthase and ATPases Research #ATP hydrolysis #ATP synthase #ATP synthase gamma subunit #ATPase #Archaea #Biochemistry #Biology #Biomolecules (q-bio.BM) #Biophysics #Chemiosmosis #Chemistry #Chloroplast #Conformational change #Enzyme #F-ATPase #FOS: Biological sciences #Fluorescence #Förster resonance energy transfer #Mitochondrial Function and Pathology #Photosynthetic Processes and Mechanisms #Protein subunit #Single-molecule FRET #Thylakoid #V-ATPase #q-bio.BM
paper · pdf · doi:10.48550/arxiv.1801.04692
published in arXiv (Cornell University) (Cornell University) · 12 pages, 6 figures
arxiv created 2018/01/15 · openalex publication_date 2018/01/15 · arxiv updated 2018/01/16 · openalex created_date 2022/10/02 · openalex updated_date 2026/07/28
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.