Coupling of rotation and catalysis in F1-ATPase revealed by single-molecule imaging and manipulation
Kengo Adachi,Kazuhiro Oiwa,Takayuki Nishizaka,Shou Furuike,Hiroyuki Noji,Hiroyasu Itoh,Masasuke Yoshida,Kazuhiko Kinosita +7 more
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TLDR
It is shown by high-speed imaging of rotation in single molecules of F(1) that phosphate release drives the last 40 degrees of the 120 degrees step, and that the 40 degrees rotation accompanies reduction of the affinity for phosphate.About:
This article is published in Cell.The article was published on 2007-07-27 and is currently open access. It has received 375 citations till now. The article focuses on the topics: ATP hydrolysis & ATPase.read more
Citations
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Dimers of mitochondrial ATP synthase form the permeability transition pore
Valentina Giorgio,Sophia von Stockum,Manuela Antoniel,Astrid Fabbro,Federico Fogolari,Michael Forte,Gary D. Glick,Valeria Petronilli,Mario Zoratti,Ildikò Szabò,Giovanna Lippe,Paolo Bernardi +11 more
TL;DR: It is shown that CyPD binds the oligomycin sensitivity-conferring protein subunit of the enzyme at the same site as the ATP synthase inhibitor benzodiazepine 423 (Bz-423), which sensitizes the PTP to Ca2+.
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Structure and mechanism of ABC transporters.
TL;DR: Recent progress with the X-ray crystal structure determination of a variety of bacterial and eukaryotic ABC transporters has helped to advance the understanding of the ATP hydrolysis-driven transport mechanism but has also illustrated the large structural and functional diversity within the family.
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The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology
Paolo Bernardi,Andrea Rasola,Andrea Rasola,Andrea Rasola,Michael Forte,Giovanna Lippe,Giovanna Lippe,Giovanna Lippe +7 more
TL;DR: Structural and functional features of F-ATP synthases are discussed that may provide clues to its transition from an energy-conserving into anEnergy-dissipating device as well as recent advances on signal transduction to the PTP and on its role in cellular pathophysiology.
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Mitochondrial ATP synthase: architecture, function and pathology
TL;DR: Questions remain to be answered regarding the structure of subunits, the function of the rotary nanomotor at a molecular level, and the human complex V assembly process, which will guide physio(patho)logical studies, paving the way for future therapeutic interventions.
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High-Speed Atomic Force Microscopy Reveals Rotary Catalysis of Rotorless F1-ATPase
TL;DR: High-speed atomic force microscopy is used to show that the rotorless F1 still “rotates”; in the isolated α3β3 stator ring, the three β subunits cyclically propagate conformational states in the counterclockwise direction, similar to the rotary shaft rotation in F1.
References
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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
TL;DR: The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
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Direct observation of the rotation of F1-ATPase
TL;DR: It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.
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Application of a Theory of Enzyme Specificity to Protein Synthesis
TL;DR: The suggestion of Lipmann' that the energy required to drive this reaction to the right came from adenosine triphosphate has been supported by the extensive work and an analysis of why this linking of amino acids presents such formidable difficulties is revealing.
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Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
TL;DR: This approach can be used directly to image single fluorescently labelled myosin molecules and detect individual ATP turnover reactions and can be applied to the study of many types of enzymes and biomolecules.