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ATP Driven Pumps I: An Overview

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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.
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Related Experiment Video

Updated: Jul 13, 2026

F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

F₁F_O ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

Published on: May 4, 2013

F1-ATPase: a highly coupled reversible rotary motor.

R Iino¹, H Noji

¹The Institute of Scientific and Industrial Research, Osaka University, Mihogaoka 8-1, Ibaraki 567-0047, Osaka, Japan.

Biochemical Society Transactions

|October 21, 2006

Summary

The epsilon subunit significantly enhances ATP synthesis in F1-ATPase molecular motors. This discovery reveals its crucial role as a coupling factor, improving efficiency from 0.3 to 2.3 ATP per turn.

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

F1-ATPase is a rotary molecular motor crucial for cellular energy production.
Understanding its coupling ratio is key to elucidating energy transduction mechanisms.

Purpose of the Study:

To investigate the coupling ratio of ATP synthesis catalyzed by single F1-ATPase molecules.
To determine the role of the epsilon subunit in modulating F1-ATPase efficiency.

Main Methods:

Utilized femtolitre reaction chamber arrays for sensitive biological reaction measurements.
Combined femtolitre chambers with rotating magnetic tweezers to study single F1-ATPase molecules.
Measured ATP synthesis rates and coupling ratios under varying conditions.

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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Isolation of F₁-ATPase from the Parasitic Protist Trypanosoma brucei

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Last Updated: Jul 13, 2026

F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

F₁F_O ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

Published on: May 4, 2013

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

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Isolation of F₁-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

Main Results:

The alpha3beta3gamma subcomplex of F1-ATPase exhibited a low coupling ratio (10%, 0.3 ATP/turn).
Reconstitution with the epsilon subunit significantly improved the coupling ratio to 77% (2.3 ATP/turn).

Conclusions:

The epsilon subunit acts as a novel coupling factor for F1-ATPase.
This finding provides new insights into the mechanism of highly coupled ATP synthesis.
The epsilon subunit plays a critical role in optimizing the efficiency of this molecular motor.