Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase

• Main Authors: Sielaff, Hendrik, Singh, Dhirendra, Grüber, Gerhard, Börsch, Michael
• Other Authors: Enderlein, Jörg
• Format: Article
• Language: English
• Published: 2018
• Subjects: Conformational Change; A1AO-ATP Synthase; DRNTU::Science::Biological sciences
• Online Access: https://hdl.handle.net/10356/88875; http://hdl.handle.net/10220/45931
• Institution: Nanyang Technological University

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 mitochon...