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Related Concept Videos

ATP Energy Storage and Release01:31

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
ATP Energy Storage and Release01:31

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
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...
Hydrolysis of ATP01:08

Hydrolysis of ATP

The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
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 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...

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Related Experiment Video

Updated: Jul 17, 2026

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
10:28

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

Published on: August 17, 2019

Enzyme-based field-effect transistor for adenosine triphosphate (ATP) sensing.

Satoshi Migita1, Kazunari Ozasa, Tomoya Tanaka

  • 1Department of Biological Functions and Engineering, Kyushu Institute of Technology, Kitakyushu Science and Research Park, Fukuoka, Japan.

Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry
|January 11, 2007
PubMed
Summary

This study introduces a novel biosensor for detecting adenosine triphosphate (ATP). The sensor utilizes an enzyme and an ion-selective field-effect transistor for accurate, in situ ATP measurements, crucial for hygiene monitoring.

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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
10:28

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Published on: August 17, 2019

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Area of Science:

  • Biotechnology
  • Biosensor Technology
  • Biochemistry

Background:

  • Adenosine triphosphate (ATP) is vital for life, serving as an energy carrier and biomarker for cellular viability.
  • Accurate in situ ATP detection is critical for applications like hygiene monitoring and bio-trace analysis.

Purpose of the Study:

  • To develop a novel biosensor for selective and sensitive in situ detection of adenosine triphosphate (ATP).
  • To integrate enzymatic activity with ion-selective field-effect transistor (ISFET) technology for ATP sensing.

Main Methods:

  • Developed an ATP sensor by immobilizing apyrase (ATP hydrolase) onto a Tantalum pentoxide (Ta2O5) ISFET gate surface using a gel matrix.
  • Utilized the proton (H+) byproduct generated from ATP dephosphorylation catalyzed by apyrase to generate a measurable electrical signal from the ISFET.

Main Results:

  • The developed biosensor demonstrated a response directly proportional to the ATP concentration in solution.
  • The ISFET-based sensor effectively detected ATP through an interfacial enzymatic reaction, producing H+ as a byproduct.

Conclusions:

  • The novel enzyme-ISFET biosensor provides a reliable method for in situ ATP measurement.
  • This technology is suitable for practical applications, particularly in hygiene monitoring and assessing biological trace indicators.