Jove
Visualize
Contact Us

Related Concept Videos

Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

2.8K
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...
2.8K
Electron Transport Chain Components01:29

Electron Transport Chain Components

1.1K
The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
1.1K
Electron Transport Chains01:28

Electron Transport Chains

114.9K
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
114.9K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.9K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.9K
The Electron Transport Chain01:30

The Electron Transport Chain

20.8K
The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
20.8K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

10.2K
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...
10.2K

You might also read

Related Articles

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

Sort by
Same author

Comprehensive evaluation of typical medical waste treatment technologies in view of environmental and economic perspectives.

Environmental research·2026
Same author

Harnessing interfacial click polymerization using pyridinium-yne films as photochromic, radical generation and sensing platforms.

Nature communications·2026
Same author

Design and synthesis of a tetraphenylethene-porphyrin hetero-faced molecular cage for photodynamic therapy.

National science review·2026
Same author

Colossal Photovoltaic Current in Ferroelectric Oxide by Constructing Defect Band.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Co Single Atom Coupled with 3D-Printed Electrodes for High-Efficiency Solar-Driven Oxygen Evolution.

ACS nano·2026
Same author

Dual-Color Tunable Circularly Polarized Luminescence With Anti-Thermal-Quenching Enabled by Asymmetric Hydrogen-Bonding Networks in Hybrid Manganese Halides.

Advanced materials (Deerfield Beach, Fla.)·2026
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 Experiment Video

Updated: Mar 11, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
05:51

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method

Published on: July 19, 2019

6.7K

Proton shuttle-assisted triplet energy transfer.

Zhaolong Wang1, Jingyi Zhu1, Kaifeng Wu2,3

  • 1State Key Laboratory of Chemical Reaction Dynamics and New Cornerstone Science Laboratory, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.

Nature Materials
|March 10, 2026
PubMed
Summary

Researchers discovered proton shuttle-assisted triplet energy transfer, a new mechanism for energy conversion. This process enhances energy transfer rates and efficiency in quantum dot systems, advancing materials science.

More Related Videos

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.5K
Integrating a Triplet-triplet Annihilation Up-conversion System to Enhance Dye-sensitized Solar Cell Response to Sub-bandgap Light
11:26

Integrating a Triplet-triplet Annihilation Up-conversion System to Enhance Dye-sensitized Solar Cell Response to Sub-bandgap Light

Published on: September 12, 2014

13.1K

Related Experiment Videos

Last Updated: Mar 11, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
05:51

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method

Published on: July 19, 2019

6.7K
Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.5K
Integrating a Triplet-triplet Annihilation Up-conversion System to Enhance Dye-sensitized Solar Cell Response to Sub-bandgap Light
11:26

Integrating a Triplet-triplet Annihilation Up-conversion System to Enhance Dye-sensitized Solar Cell Response to Sub-bandgap Light

Published on: September 12, 2014

13.1K

Area of Science:

  • Materials Science
  • Photochemistry
  • Energy Conversion

Background:

  • Proton transfer coupled with electronic transitions is crucial for energy materials.
  • Existing mechanisms include proton-coupled electron transfer and singlet energy transfer.
  • Triplet energy transfer mechanisms remain largely unexplored.

Purpose of the Study:

  • To report a novel mechanism: proton shuttle-assisted triplet energy transfer.
  • To investigate its role in ZnSe-based quantum dot systems with phenol-pyridine acceptors.
  • To understand how proton transfer influences triplet energy migration.

Main Methods:

  • Utilized ultrafast spectroscopic measurements.
  • Employed kinetic isotope effect studies.
  • Investigated ZnSe quantum dots functionalized with phenol-pyridine dyadic acceptors.

Main Results:

  • Photoexcitation of ZnSe initiates coupled hole and proton transfer.
  • Subsequent electron transfer and back proton transfer facilitate triplet energy migration.
  • A trifluoromethyl substituent on pyridine alters the transfer sequence.
  • The proton shuttle significantly boosts energy transfer rate and efficiency.

Conclusions:

  • Proton shuttle-assisted triplet energy transfer is a viable mechanism for efficient energy migration.
  • This mechanism offers new pathways for designing advanced energy conversion and storage materials.
  • Modulating proton transfer dynamics can control energy transfer processes.