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

Electron Transport Chains01:28

Electron Transport Chains

111.1K
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...
111.1K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

18.2K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
18.2K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.9K
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...
8.9K
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

16.0K
The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
16.0K
Electron Carriers01:24

Electron Carriers

91.0K
Electron carriers can be thought of as electron shuttles. These compounds can easily accept electrons (i.e., be reduced) or lose them (i.e., be oxidized). They play an essential role in energy production because cellular respiration is contingent on the flow of electrons.
Over the many stages of cellular respiration, glucose breaks down into carbon dioxide and water. Electron carriers pick up electrons lost by glucose in these reactions, temporarily storing and releasing them into the electron...
91.0K
Electron Transport Chain Components01:29

Electron Transport Chain Components

779
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...
779

You might also read

Related Articles

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

Sort by
Same author

Efficacy and safety of compound Qingdai enema in rapidly alleviating inflammatory activity in ulcerative colitis: a prospective study.

Frontiers in pharmacology·2026
Same author

IL17 signaling promotes oocyte developmental competence acquisition during maturation.

Cellular & molecular biology letters·2026
Same author

Structural insights into OSTα/β-mediated transport of bile acids and steroid conjugates.

Nature structural & molecular biology·2026
Same author

Liquid Chromatographic Methods for Microsampling in Sports Drug Monitoring: Progress in DBS and VAMS.

Biomedical chromatography : BMC·2026
Same author

Low CO<sub>2</sub> Responsive Gene Co-Expression Network Identifies Regulators Facilitating Photosynthetic Growth of Synechocystis sp. Strain PCC 6803.

Plant, cell & environment·2026
Same author

Titrated Contrast Recanalization: A Novel Controlled-Contrast Technique for Anterograde Crossing of Chronic Total Occlusion.

The American journal of cardiology·2026

Related Experiment Video

Updated: Dec 28, 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

10.6K

Structural insights into NDH-1 mediated cyclic electron transfer.

Chunli Zhang1,2,3, Jin Shuai4,5, Zhaoxing Ran6

  • 1Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, 200125, Shanghai, China.

Nature Communications
|February 16, 2020
PubMed
Summary
This summary is machine-generated.

This study reveals the structure of the ferredoxin-NDH-1L complex, crucial for cyclic electron transfer (PSI CET) in cyanobacteria. It uncovers how specific subunits help manage high-light stress for survival.

More Related Videos

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.5K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.6K

Related Experiment Videos

Last Updated: Dec 28, 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

10.6K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.5K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.6K

Area of Science:

  • Photosynthesis research
  • Structural biology
  • Cyanobacterial metabolism

Background:

  • Cyclic electron transfer around photosystem I (PSI CET) is vital for photosynthesis and antioxidant defense.
  • NDH-1 is a key protein complex in the PSI CET pathway.
  • Understanding NDH-1 structure and regulation is crucial for photosynthesis efficiency.

Purpose of the Study:

  • To determine the high-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex.
  • To elucidate the roles of regulatory subunits in NDH-1 function under high-light stress.
  • To understand the hierarchical mechanism for cyanobacterial survival in aerobic environments.

Main Methods:

  • 3.2-Å-resolution cryo-electron microscopy (cryo-EM).
  • Structural analysis of the ferredoxin-NDH-1L complex from Thermosynechococcus elongatus.
  • Investigating the roles of specific subunits (NdhV, NdhS, NdhO, NdhL) in PSI CET.

Main Results:

  • The cryo-EM structure reveals associated beta-carotene and lipid molecules within NDH-1L.
  • Regulatory subunits NdhV, NdhS, and NdhO are located near the Fd-binding site.
  • NdhV facilitates Fd binding and accelerates PSI CET under short-term high light; NDH-1MS complex forms under prolonged high light.

Conclusions:

  • The NDH-1 complex, with its specific subunits, plays a critical role in adapting to high-light stress.
  • NdhV's role in Fd binding and the formation of NDH-1MS under prolonged stress highlight a hierarchical regulatory mechanism.
  • This mechanism is essential for cyanobacterial survival in fluctuating light and aerobic conditions.