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Related Concept Videos

ATP Driven Pumps I: An Overview01:27

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 are...
ATP Synthase: Mechanism01:48

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 ATP...
ATP Synthase: Structure01:18

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 Driven Pumps II: P-type Pumps01:34

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...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Chemiosmosis and ATP Synthesis01:22

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...

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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
08:21

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F1-ATPase: a highly efficient rotary ATP machine.

K Kinosita1, R Yasuda, H Noji

  • 1Department of Physics, Faculty of Science and Technology, Keio University, Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.

Essays in Biochemistry
|December 11, 2002
PubMed
Summary

The F1-ATPase molecular motor operates with 120-degree steps, maintaining constant torque and efficiency. This rotary motor converts chemical energy from ATP hydrolysis into mechanical work with near 100% efficiency.

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Last Updated: Jul 13, 2026

F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes
08:21

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Published on: May 4, 2013

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • F1-ATPase functions as a rotary motor at the molecular level.
  • It comprises a central gamma subunit rotating within an alpha3 beta3 hexamer stator.

Purpose of the Study:

  • To investigate the mechanical properties and efficiency of the F1-ATPase molecular motor.
  • To understand the relationship between ATP hydrolysis and mechanical work output.

Main Methods:

  • Observation of single F1-ATPase molecule rotation.
  • Measurement of torque and mechanical work at discrete steps.
  • Analysis of efficiency under varying load and speed conditions.

Main Results:

  • The motor operates in discrete 120-degree steps.
  • Constant torque of 40 pN.nm is produced over a range of conditions.
  • Mechanical work per ATP is 80-90 pN.nm, near the free energy of ATP hydrolysis.

Conclusions:

  • F1-ATPase operates with remarkable efficiency, approaching 100%.
  • The motor's consistent performance highlights its effectiveness in energy transduction.