Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

ATP Synthase: Structure

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...

ATP Synthase: Mechanism

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...

Chemiosmosis and ATP Synthesis

Chemiosmosis and ATP Synthesis

The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...

ATP Driven Pumps I: An Overview

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...

Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

ATP Driven Pumps II: P-type Pumps

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Catalytic dwell oscillations complete the F<sub>1</sub>-ATPase mechanism.

Communications chemistry·2025

Same author

Eukaryotic yeast V<sub>1</sub>-ATPase rotary mechanism insights revealed by high-resolution single-molecule studies.

Frontiers in molecular biosciences·2024

Same author

pH-dependent 11° F<sub>1</sub>F<sub>O</sub> ATP synthase sub-steps reveal insight into the F<sub>O</sub> torque generating mechanism.

eLife·2021

Same author

ΩqPCR measures telomere length from single-cells in base pair units.

Nucleic acids research·2021

Same author

Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.

Molecules (Basel, Switzerland)·2019

Same author

Elastic coupling power stroke mechanism of the F<sub>1</sub>-ATPase molecular motor.

Proceedings of the National Academy of Sciences of the United States of America·2018

Search research articles

Related Experiment Video

Updated: Aug 29, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

F₁F_O ATP synthase molecular motor mechanisms.

Wayne D Frasch¹, Zain A Bukhari¹, Seiga Yanagisawa¹

¹School of Life Sciences, Arizona State University, Tempe, AZ, United States.

Frontiers in Microbiology

|September 9, 2022

Summary

The F-ATP synthase enzyme uses proton flow to rotate its c-ring, driving ATP synthesis. This rotation involves specific proton translocation steps and electrostatic interactions, revealing the mechanism of energy conversion.

Keywords:

F1 ATPase F1Fo ATP synthase rotary molecular motor single-molecule studies torque

More Related Videos

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Related Experiment Videos

Last Updated: Aug 29, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Area of Science:

Biochemistry
Molecular Biology
Bioenergetics

Background:

F-ATP synthase synthesizes ATP using F1 and FO motors.
The FO complex includes a c-ring that rotates with proton flow.
Single-molecule studies have investigated the rotation mechanism.

Purpose of the Study:

To elucidate the mechanism of proton translocation and rotation in F-ATP synthase.
To understand the role of c-ring rotation in ATP synthesis.
To investigate the influence of protonation states and electrostatic interactions.

Main Methods:

Single-molecule studies of F1FO in lipid bilayer nanodisks.
Arrhenius analysis of F1 rotation.
Site-directed mutagenesis of FO subunit-a residues.
pKa determination of conserved carboxyl groups.

Main Results:

The c-ring rotation is coupled to proton translocation in 11° steps.
Protonation/deprotonation by subunit-a residues influences c-ring rotation.
Mutations altering pKa values proportionally affected the 11° rotation.
A mechanism involving Grotthuss proton translocation and electrostatic interactions was supported.

Conclusions:

Proton translocation occurs during the 11° steps of c-ring rotation.
The FO motor utilizes a Grotthuss mechanism for proton translocation.
Electrostatic interactions drive the remaining rotation for ATP synthesis.