Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

ATP Energy Storage and Release01:31

ATP Energy Storage and Release

11.3K
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...
11.3K
Hydrolysis of ATP01:08

Hydrolysis of ATP

76.9K
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...
76.9K
ATP and Energy Production01:23

ATP and Energy Production

369
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...
369
Coupled Reactions01:17

Coupled Reactions

8.4K
Cellular processes such as building and breaking down complex molecules occur through stepwise chemical reactions. Some of these chemical reactions are spontaneous and release energy, whereas others require energy to proceed. Cells often couple the energy-releasing reaction with the energy-requiring one to carry out important cell functions. 
Energy in adenosine triphosphate or ATP molecules is easily accessible to do work. ATP powers the majority of energy-requiring cellular reactions....
8.4K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.2K
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...
15.2K
ATP Synthase: Structure01:18

ATP Synthase: Structure

13.1K
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...
13.1K

You might also read

Related Articles

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

Sort by
Same author

Excitation of NH Stretching Modes in Aromatic Molecules: <i>o</i>-Toluidine and α-Methylbenzylamine.

The journal of physical chemistry. B·2023
Same author

Influence of a Methyl Group on the Unidirectional Flow of Vibrational Energy in an Adenine-Thymine Base Pair.

The journal of physical chemistry. B·2023
Same author

Intramolecular vibrational energy redistribution in nucleobases: Excitation of NH stretching vibrations in adenine-uracil + H<sub>2</sub>O.

The Journal of chemical physics·2022
Same author

Inter- and Intramolecular Vibrational Energy Flow in a Formamide-Water Complex.

The journal of physical chemistry. A·2020
Same author

Relaxation of the H<sub>2</sub>O Overtone Bending Vibration in the Water Dimer···Hydroxyl Radical Complex.

The journal of physical chemistry. A·2018
Same author

Energy Transfer to the Hydrogen Bond in the (H<sub>2</sub>O)<sub>2</sub> + H<sub>2</sub>O Collision.

The journal of physical chemistry. B·2017

Related Experiment Video

Updated: Sep 12, 2025

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
07:25

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

Published on: October 17, 2014

15.7K

Vibrational energy flow in adenosine triphosphate.

H K Shin1

  • 1Department of Chemistry, University of Nevada, Reno, Nevada 89557, USA.

The Journal of Chemical Physics
|August 4, 2025
PubMed
Summary

Water molecules efficiently transfer vibrational energy to adenosine triphosphate (ATP). This energy rapidly redistributes throughout ATP, primarily to high-frequency bonds, within a picosecond.

Area of Science:

  • Physical Chemistry
  • Biophysics
  • Molecular Dynamics

Background:

  • Understanding energy transfer in biological systems is crucial for elucidating molecular mechanisms.
  • Adenosine triphosphate (ATP) is the primary energy currency of cells, and its interactions with other molecules are fundamental.
  • Vibrational energy transfer dynamics play a key role in biochemical processes.

Purpose of the Study:

  • To investigate intermolecular vibrational energy transfer from water (H2O) to adenosine triphosphate (ATP).
  • To analyze intramolecular energy redistribution within ATP following energy transfer.
  • To elucidate the pathways and timescales of energy flow in the H2O-ATP system.

Main Methods:

  • Employed semiclassical Wentzel-Kramers-Brillouin (WKB) procedure.

More Related Videos

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

18.3K
High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers
09:53

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers

Published on: October 26, 2021

4.9K

Related Experiment Videos

Last Updated: Sep 12, 2025

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
07:25

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

Published on: October 17, 2014

15.7K
Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

18.3K
High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers
09:53

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers

Published on: October 26, 2021

4.9K
  • Utilized quasiclassical trajectory calculations to simulate molecular dynamics.
  • Focused on hydrogen bond interactions between excited H2O and ATP's gamma-phosphate group.

    • Main Results:

    • Identified efficient intermolecular energy flow from excited H2O (symmetric stretch) to ATP via hydrogen bonding.
    • Observed rapid intramolecular energy redistribution within ATP, primarily to OH, CH, and NH bonds.
    • Demonstrated that the phosphorus-oxygen chain acts as an efficient conduit for energy distribution to ribose and adenine moieties on a sub-picosecond timescale.

    Conclusions:

    • Intermolecular vibrational energy transfer from H2O to ATP is efficient, driven by hydrogen bond interactions.
    • ATP exhibits rapid intramolecular energy redistribution, distributing energy broadly across high-frequency bonds.
    • The observed energy transfer and redistribution dynamics occur on ultrafast timescales (sub-picosecond to picosecond).