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

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

Electron Transport Chain: Complex I and II

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...
Electron Transport Chains01:28

Electron Transport Chains

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...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

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...
The Electron Transport Chain01:30

The Electron Transport Chain

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 in...
Electron Transport Chain Components01:29

Electron Transport Chain Components

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...

You might also read

Related Articles

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

Sort by
Same author

Evidence for the Collective Nature of Radial Flow in Pb+Pb Collisions with the ATLAS Detector.

Physical review letters·2026
Same author

Evidence for the Dimuon Decay of the Higgs Boson in pp Collisions with the ATLAS Detector.

Physical review letters·2025
Same author

Evidence for Longitudinally Polarized W Bosons in the Electroweak Production of Same-Sign W Boson Pairs in Association with Two Jets in pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2025
Same author

Observation of tt[over ¯] Production in Pb+Pb Collisions at sqrt[s_{NN}]=5.02  TeV with the ATLAS Detector.

Physical review letters·2025
Same author

Search for Dark Matter Produced in Association with a Dark Higgs Boson in the bb[over ¯] Final State Using pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2025
Same author

Search for Magnetic Monopole Pair Production in Ultraperipheral Pb+Pb Collisions at sqrt[s_{NN}]=5.36  TeV with the ATLAS Detector at the LHC.

Physical review letters·2025
Same journal

Geometrical isomerization of hydroxycinnamic acid under UV-light: Structural plasticity as a driver of metabolite complexity.

Photochemistry and photobiology·2026
Same journal

Photochemistry of CryB from Rhodobacter sphaeroides.

Photochemistry and photobiology·2026
Same journal

Artemisitene formation during UVA-assisted Fenton oxidation of arteannuin B.

Photochemistry and photobiology·2026
Same journal

Surface alteration of Candida albicans after antifungal photodynamic therapy: A Raman spectroscopic study.

Photochemistry and photobiology·2026
Same journal

Phototherapies mediated by metallic nanoparticles and near-infrared radiation in skin cancer: A systematic review.

Photochemistry and photobiology·2026
Same journal

The burning question: Does exposure to low dose and low irradiance ultraviolet radiation lead to cutaneous DNA damage in people with skin types I-III?

Photochemistry and photobiology·2026
See all related articles

Related Experiment Video

Updated: Jun 27, 2026

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

Structure-function of the cytochrome b6f complex.

D Baniulis1, E Yamashita, H Zhang

  • 1Department of Biological Sciences, Purdue University, West Lafayette, IN, USA.

Photochemistry and Photobiology
|December 11, 2008
PubMed
Summary
This summary is machine-generated.

Recent crystal structures reveal the cytochrome b6f complex as a dimeric protein. Heme c(n) is implicated as an n-side plastoquinone reductase, suggesting a branch point for electron transport pathways.

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

Related Experiment Videos

Last Updated: Jun 27, 2026

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

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

Area of Science:

  • Photosynthesis research
  • Protein complex structure and function
  • Bioenergetics

Background:

  • The cytochrome b6f complex is crucial for electron and proton transfer in oxygenic photosynthesis.
  • Recent crystal structures provide high-resolution insights into its dimeric organization and subunit composition.
  • Understanding its mechanism is key to deciphering energy conversion in photosynthetic organisms.

Purpose of the Study:

  • To analyze the structure and function of the cytochrome b6f complex using recent crystal structures.
  • To investigate the role of heme c(n) in electron transfer pathways.
  • To explore evolutionary conservation and unresolved questions regarding complex dynamics.

Main Methods:

  • Analysis of crystal structures from Mastigocladus laminosus and Chlamydomonas reinhardtii.
  • Discussion of proteolysis challenges during cyanobacterial complex crystallization.
  • Comparative analysis of cytochrome b6f and bc1 complexes.

Main Results:

  • The cytochrome b6f complex is a symmetric dimeric complex with eight subunits.
  • Heme c(n) is identified as a ligand for quinone analogue inhibitors, suggesting its role in plastoquinone reduction.
  • Conservation of key domains indicates evolutionary links between cytochrome b6f and bc1 complexes.

Conclusions:

  • Heme c(n) and heme b(n) may define a branch point in bc complexes, supporting diverse electron transport pathways.
  • Further research is needed to elucidate the shuttle mechanisms of the Rieske [2Fe-2S] protein and quinone/plastoquinol.
  • The role of the n-side of the b6f complex in regulating electron transfer rates requires further investigation.