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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

14.9K
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...
14.9K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.5K
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...
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Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

1.7K
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...
1.7K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

9.6K
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...
9.6K
ATP and Energy Production01:23

ATP and Energy Production

1.4K
Adenosine triphosphate (ATP) is a critical molecule that functions as the main energy carrier in cells. Structurally, ATP consists of an adenosine molecule—comprising adenine and ribose—bonded to three phosphate groups. The high-energy bonds between these phosphate groups store significant amounts of potential energy. This energy is released during hydrolysis, wherein ATP is converted to adenosine diphosphate (ADP) or adenosine monophosphate (AMP), driving a variety of essential...
1.4K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

4.6K
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...
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Related Experiment Video

Updated: Jan 5, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

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ATP Synthase: Expression, Purification, and Function.

Meghna Sobti1, Robert Ishmukhametov2, Alastair G Stewart3

  • 1The Victor Chang Cardiac Research Institute, Darlinghurst, NSW, Australia.

Methods in Molecular Biology (Clifton, N.J.)
|October 16, 2019
PubMed
Summary
This summary is machine-generated.

This study details methods for producing and testing Escherichia coli ATP synthase, a crucial enzyme for cellular energy. Researchers purified and assessed the function of this vital rotary motor protein.

Keywords:
ATP synthaseATPaseBioenergeticsEnzymeRotary motor

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

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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Related Experiment Videos

Last Updated: Jan 5, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • ATP synthase is a universally conserved enzyme responsible for cellular energy production.
  • It operates through a complex rotary catalytic mechanism essential for life.
  • Understanding its function requires robust methods for isolation and analysis.

Purpose of the Study:

  • To provide detailed protocols for the expression and purification of E. coli ATP synthase.
  • To outline methods for the functional assessment of purified E. coli ATP synthase.
  • To facilitate further research into the rotary catalytic mechanism of ATP synthase.

Main Methods:

  • Bacterial expression of E. coli ATP synthase.
  • Multi-step purification techniques including chromatography.
  • In vitro functional assays to assess enzymatic activity.

Main Results:

  • Successfully expressed and purified active E. coli ATP synthase.
  • Established reliable methods for assessing enzyme function.
  • Characterized key properties of the purified enzyme.

Conclusions:

  • The described methods enable robust study of E. coli ATP synthase.
  • These protocols are valuable for researchers investigating energy production mechanisms.
  • Further elucidation of ATP synthase's rotary mechanism is now more accessible.