Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
نویسندگان
چکیده
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 of ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer demonstrated that the C-terminus of rotary subunit in Escherichia coli 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 signals and potential artefacts.
منابع مشابه
Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer.
Elastic conformational changes of the protein backbone are essential for catalytic activities of enzymes. To follow relative movements within the protein, Förster-type resonance energy transfer (FRET) between two specifically attached fluorophores can be applied. FRET provides a precise ruler between 3 and 8nm with subnanometer resolution. Corresponding submillisecond time resolution is suffici...
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