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 Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

7.7K
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...
7.7K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.5K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.5K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

14.6K
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...
14.6K
The Electron Transport Chain01:30

The Electron Transport Chain

17.0K
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...
17.0K
Electron Transport Chains01:28

Electron Transport Chains

100.2K
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...
100.2K
Anoxygenic Photosynthesis01:30

Anoxygenic Photosynthesis

55
Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
55

You might also read

Related Articles

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

Sort by
Same author

Deciphering the Mto electron uptake pathway of <i>Sideroxydans lithotrophicus</i> ES-1.

Applied and environmental microbiology·2026
Same author

Iron binding before iron limitation: siderophore synthesis arose well before iron became a limiting element.

ISME communications·2026
Same author

Caspofungin binding to iron compromises its antifungal efficacy against Candida albicans.

Communications biology·2025
Same author

Polyphasic discrimination of <i>Shewanella seohaensis</i> from closely related species and a whole-genome multilocus (wgMLST) scheme for the evaluation of diversity within this <i>Shewanella</i> clade.

Applied and environmental microbiology·2025
Same author

Injectable and implantable hydrogels for localized delivery of drugs and nanomaterials for cancer chemotherapy: A review.

International journal of pharmaceutics·2025
Same author

Flavin-containing siderophore-interacting protein of Shewanella putrefaciens DSM 9451 reveals common structural and functional aspects of ferric-siderophore reduction.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2025

Related Experiment Video

Updated: Jul 31, 2025

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

4.8K

Exploring substrate interaction in respiratory alternative complex III from Rhodothermus marinus.

Filipa Calisto1, Smilja Todorovic2, Ricardo O Louro2

  • 1University of Lisbon, Faculty of Sciences, Department of Chemistry and Biochemistry and BioISI - Biosystems & Integrative Sciences Institute, Campo Grande, C8, 1749-016 Lisboa, Portugal.

Biochimica Et Biophysica Acta. Bioenergetics
|May 1, 2023
PubMed
Summary

Rhodothermus marinus possesses a unique Alternative Complex III (ACIII) for respiration at high temperatures. This study used nanodiscs to investigate ACIII

Keywords:
Alternative complex III (ACIII)Cytochrome bc1High Potential Iron Sulfur Protein (HiPIP)MenaquinoneRespiratory chainThermophile

More Related Videos

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

1.9K
High-resolution Respirometry to Assess Mitochondrial Function in Permeabilized and Intact Cells
08:33

High-resolution Respirometry to Assess Mitochondrial Function in Permeabilized and Intact Cells

Published on: February 8, 2017

41.6K

Related Experiment Videos

Last Updated: Jul 31, 2025

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

4.8K
Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

1.9K
High-resolution Respirometry to Assess Mitochondrial Function in Permeabilized and Intact Cells
08:33

High-resolution Respirometry to Assess Mitochondrial Function in Permeabilized and Intact Cells

Published on: February 8, 2017

41.6K

Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Rhodothermus marinus is a thermohalophilic bacterium thriving at 65°C.
  • Its microaerobic metabolism is optimized for extreme conditions.
  • A novel quinone:cytochrome c oxidoreductase, Alternative Complex III (ACIII), distinct from the bc1 complex, has been identified.

Purpose of the Study:

  • To investigate the activity and function of Alternative Complex III (ACIII) in a membrane-mimicking environment.
  • To elucidate the interactions of ACIII with its substrates and electron acceptors.

Main Methods:

  • Utilized nanodiscs and liposomes to create membrane-mimicking systems.
  • Studied the enzymatic activity of ACIII in these reconstituted systems.
  • Investigated the interaction of ACIII with menaquinone, HiPIP, cytochrome c, and the caa3 oxygen reductase.

Main Results:

  • ACIII activity was successfully reconstituted and studied in nanodiscs and liposomes.
  • The interaction of ACIII with menaquinone and its electron acceptors was characterized.
  • The interplay between ACIII and the caa3 oxygen reductase was explored.

Conclusions:

  • Alternative Complex III (ACIII) plays a significant role in the respiratory chain of Rhodothermus marinus.
  • Membrane-mimicking systems are effective for studying ACIII function.
  • Further research into ACIII provides insights into microbial adaptation to extreme environments.