ArticleProceedings of the National Academy of Sciences of the United States of America2005
ATP-driven stepwise rotation of FoF1-ATP synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 157 citations in OpenAlex.
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- ATP synthesis of Enterococcus hirae V-ATPase driven by sodium motive force.The Journal of biological chemistry · 2025Article
- FPharmaceutics · 2023Article
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- Single molecule kinetics of bacteriorhodopsin by HS-AFM.Nature communications · 2021Article
- The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2021Article
- Minimal physicalism as a scale-free substrate for cognition and consciousness.Neuroscience of consciousness · 2021Article
- Droplet-Based Microfluidic High Throughput Screening ofFrontiers in bioengineering and biotechnology · 2021Article
- Controlling the Revolving and Rotating Motion Direction of Asymmetric Hexameric Nanomotor by Arginine Finger and Channel Chirality.ACS nano · 2019Review
- Using a system's equilibrium behavior to reduce its energy dissipation in nonequilibrium processes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Structure of the mitochondrial ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2016Article
- Thermodynamics and kinetics of the FoF1-ATPase: application of the probability isotherm.Royal Society open science · 2016Article
- A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective.Photosynthesis research · 2015Article
- Torque generation of Enterococcus hirae V-ATPase.The Journal of biological chemistry · 2014Article
- Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity.Nature communications · 2014Article
- Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.Journal of biomolecular NMR · 2014Article
- Single-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimide.The Journal of biological chemistry · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FoF1-ATP synthase (FoF1) is a motor enzyme that couples ATP synthesis/hydrolysis with a transmembrane proton translocation. F1, a water-soluble ATPase portion of FoF1, rotates by repeating ATP-waiting dwell, 80 degrees substep rotation, catalytic dwell, and 40 degrees -substep rotation. Compared with F1, rotation of FoF1 has yet been poorly understood, and, here, we analyzed ATP-driven rotations of FoF1. Rotation was probed with an 80-nm bead attached to the ring of c subunits in the immobilized FoF1 and recorded with a submillisecond fast camera. The rotation rates at various ATP concentrations obeyed the curve defined by a Km of approximately 30 microM and a Vmax of approximately 350 revolutions per second (at 37 degrees C). At low ATP, ATP-waiting dwell was seen and the kon-ATP was estimated to be 3.6 x 10(7) M(-1) x s(-1). At high ATP, fast, poorly defined stepwise motions were observed that probably reflect the catalytic dwells. When a slowly hydrolyzable substrate, adenosine 5'-[gamma-thio]triphosphate, was used, the catalytic dwells consisting of two events were seen more clearly at the angular position of approximately 80 degrees . The rotational behavior of FoF1 resembles that of F1. This finding indicates that "friction" in Fo motor is negligible during the ATP-driven rotation. Tributyltin chloride, a specific inhibitor of proton translocation, slowed the rotation rate by 96%. However, dwells at clearly defined angular positions were not observed under these conditions, indicating that inhibition by tributyltin chloride is complex.
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