Subunit Movements in Single Membrane-bound H+-ATP Synthases from Chloroplasts during ATP Synthesis
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
2. Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism
3. The binding change mechanism for ATP synthase — Some probabilities and possibilities
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1. Rotation of the γ-subunit in single membrane-bound H+-ATP synthases from chloroplasts during ATP synthesis;Advances in Botanical Research;2020
2. Binding of the immunomodulatory drug Bz-423 to mitochondrial FoF1-ATP synthase in living cells by FRET acceptor photobleaching;Multiphoton Microscopy in the Biomedical Sciences XVI;2016-03-14
3. The Structure of ATPsynthases in Photosynthesis and Respiration;The Structural Basis of Biological Energy Generation;2014
4. Microscopy of single FoF1-ATP synthases- The unraveling of motors, gears, and controls;IUBMB Life;2013-02-04
5. Elastic deformations of the rotary double motor of single FoF1-ATP synthases detected in real time by Förster resonance energy transfer;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2012-10
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