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 Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.3K
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...
8.3K
Electron Transport Chain Components01:29

Electron Transport Chain Components

55
The electron transport chain is a crucial metabolic pathway facilitating energy conversion in prokaryotic and eukaryotic cells. The ETC comprises four membrane-associated protein complexes that mediate a series of redox reactions located in the inner mitochondrial membrane of eukaryotes and the plasma membrane of prokaryotes. These complexes function by transferring electrons from electron donors, such as NADH and FADH2, to terminal electron acceptors, including oxygen in aerobic respiration...
55
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

57
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...
57
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

7.6K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
7.6K
The Electron Transport Chain01:30

The Electron Transport Chain

16.9K
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...
16.9K
Electron Transport Chains01:28

Electron Transport Chains

99.6K
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...
99.6K

You might also read

Related Articles

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

Sort by
Same author

Does <i>sod1</i> encode a molecular clock? Mutations that mimic asparagine deamidation inhibit heterodimerization with ALS-mutant SOD1.

RSC chemical biology·2026
Same author

Heteroaggregation of Wild-Type and ALS Mutant SOD1.

ACS chemical neuroscience·2025
Same author

Proton-coupled electron transfer at a mis-metalated zinc site detected with protein charge ladders.

Physical chemistry chemical physics : PCCP·2024
Same author

Heat-induced structural and chemical changes to a computationally designed miniprotein.

Protein science : a publication of the Protein Society·2024
Same author

Universal pictures: A lithophane codex helps teenagers with blindness visualize nanoscopic systems.

Science advances·2024
Same author

Oxidation of Dueling Cysteine Promotes Subunit Exchange in SOD1.

ACS chemical neuroscience·2023
Same journal

Linker Engineering toward NIR-II Metal-Organic Framework with Maximal Emission beyond 1000 nm for Inflammatory Bowel Disease Imaging.

Journal of the American Chemical Society·2026
Same journal

Observing Kinetic Selectivity in Anthracene Photodimerization through Selective Quenching by Excited States of Proximate Rare Earth Cations.

Journal of the American Chemical Society·2026
Same journal

Sequence-Dependent Folding of Recognition-Encoded Melamine Oligomers.

Journal of the American Chemical Society·2026
Same journal

Large Thermo- and Mechanosalient Actuation via Cooperative Twist Elasticity-Induced Packing Motif Conversion.

Journal of the American Chemical Society·2026
Same journal

Discovery and Biosynthesis of Lanthipeptides Featuring an Azepinoindole Scaffold by Radical <i>S</i>-Adenosylmethionine Enzyme-Catalyzed C-C Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Enantiopurity-Controlled Magnetism in a Two-Dimensional Organic-Inorganic Material.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Jul 22, 2025

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
09:00

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1

Published on: April 16, 2018

10.1K

Charge Regulation in a Rieske Proton Pump Pinpoints Zero, One, and Two Proton-Coupled Electron Transfer.

Jordan C Koone1, Mikaela Simmang2, Devin L Saenger2

  • 1Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76706, United States.

Journal of the American Chemical Society
|July 24, 2023
PubMed
Summary
This summary is machine-generated.

Researchers quantified net charge changes during electron transfer (ΔZET) in Rieske proteins. They found distinct charge states supporting electron transfer (ET), proton-coupled electron transfer (PCET), and two-proton-coupled electron transfer (2PCET) mechanisms.

More Related Videos

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

10.6K
A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins
08:09

A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins

Published on: January 7, 2019

8.9K

Related Experiment Videos

Last Updated: Jul 22, 2025

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
09:00

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1

Published on: April 16, 2018

10.1K
Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

10.6K
A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins
08:09

A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins

Published on: January 7, 2019

8.9K

Area of Science:

  • Biochemistry
  • Bioenergetics
  • Protein Electrochemistry

Background:

  • Measuring net charge changes during electron transfer (ΔZET) in proteins is challenging.
  • ΔZET values are crucial for understanding electron transfer (ET) versus proton-coupled electron transfer (PCET) mechanisms.
  • Rieske [2Fe-2S] proteins are key components in biological electron transport chains.

Purpose of the Study:

  • To determine the degree of net charge regulation by proton pumps during electron transfer (ΔZET).
  • To distinguish between electron transfer (ET) and proton(s)-coupled electron transfer (PCET) in Rieske proteins.
  • To investigate the pH-dependent mechanism of proton pumping in a Rieske [2Fe-2S] subunit.

Main Methods:

  • Synthesis of protein 'charge ladders' from a Rieske [2Fe-2S] subunit of *Thermus thermophilus* (trunc*Tt*Rp).
  • Performed 120 electrostatic measurements of ΔZET across a range of pH values.
  • Correlated redox potentials with protonation energies and ΔZET values.

Main Results:

  • At pH 6.0, trunc*Tt*Rp exhibited a ΔZET of -1.01 ± 0.14, consistent with single ET.
  • At pH 8.8, trunc*Tt*Rp showed an isoelectric ΔZET of -0.01 ± 0.45, indicating PCET.
  • At pH 10.6, trunc*Tt*Rp displayed a ΔZET of +1.37 ± 0.60, consistent with two-proton-coupled ET (2PCET).
  • Observed ΔZET changes were attributed to the protonation of histidines H154 and H134.

Conclusions:

  • The study provides direct electrostatic measurements (ΔZET) for Rieske proteins across pH.
  • Findings support a discrete proton pumping mechanism involving Fe-coordinating histidines in Rieske proteins.
  • Demonstrated pH-dependent transitions between ET, PCET, and 2PCET mechanisms in trunc*Tt*Rp.