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

6.7K
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...
6.7K
Electron Transport Chains01:28

Electron Transport Chains

85.6K
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...
85.6K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

11.9K
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...
11.9K
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

9.3K
There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
9.3K
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

11.8K
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...
11.8K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.3K
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...
2.3K

You might also read

Related Articles

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

Sort by
Same author

Cardiac Computed Tomography for Atrial Fibrillation Patients Undergoing Ablation: Implications for the Prediction of Early Recurrence.

Journal of thoracic imaging·2019
Same author

The genetics of human personality.

Genes, brain, and behavior·2017
Same author

An initial investigation of associations between dopamine-linked genetic variation and smoking motives in African Americans.

Pharmacology, biochemistry, and behavior·2015
Same author

NCAM1-TTC12-ANKK1-DRD2 variants and smoking motives as intermediate phenotypes for nicotine dependence.

Psychopharmacology·2014
Same author

A randomised controlled trial of complete denture impression materials.

Journal of dentistry·2014
Same author

Synthesis and assembly of the cytochrome b-f complex in higher plants.

Photosynthesis research·2014
Same journal

Energy quenching via triplet-excited state formation of glycosylated carotenoids in the photosynthetic reaction center complex of the green sulfur bacterium Chlorobaculum tepidum.

Photosynthesis research·2026
Same journal

Quantitative phosphoproteomics profiling reveals the regulatory mechanisms underlying high light stress in maize and rice.

Photosynthesis research·2026
Same journal

Siphonous green macroalgae with contrasting capacities for the energy-dependent quenching, qE, rely on different photoprotective mechanisms.

Photosynthesis research·2026
Same journal

On the unidirectionality of electron transfer in reaction centers of Chloroflexus aurantiacus.

Photosynthesis research·2026
Same journal

The contribution of the <sup>240</sup>Ala:Glu:Glu:Thr<sup>243</sup> sequence in the DE-loop of D2 to the acceptor side of Photosystem II.

Photosynthesis research·2026
Same journal

Quick conversions and de novo synthesis within the entire α- and β-carotenoid branches during non-steady-state light transients.

Photosynthesis research·2026
See all related articles

Related Experiment Video

Updated: May 4, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
06:26

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria

Published on: November 10, 2021

4.0K

Cytochrome f: Structure, function and biosynthesis.

J C Gray1

  • 1Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK.

Photosynthesis Research
|January 11, 2014
PubMed
Summary
This summary is machine-generated.

Cytochrome f, a key component of the cytochrome bf complex, facilitates electron transfer in thylakoid membranes. Its structure and interaction with plastocyanin are crucial for photosynthesis.

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

11.5K
Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

11.4K

Related Experiment Videos

Last Updated: May 4, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
06:26

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria

Published on: November 10, 2021

4.0K
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

11.5K
Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

11.4K

Area of Science:

  • Plant Biology
  • Photosynthesis Research
  • Membrane Protein Structure

Background:

  • Cytochrome f is an essential intrinsic membrane protein within the cytochrome bf complex.
  • It plays a vital role in electron transport, connecting the Rieske FeS protein to plastocyanin in the thylakoid lumen.
  • The protein features a transmembrane anchor and a globular domain extending into the lumen.

Purpose of the Study:

  • To elucidate the structural and functional aspects of cytochrome f in photosynthetic electron transport.
  • To understand the molecular interactions between cytochrome f and plastocyanin.
  • To investigate the synthesis and targeting of cytochrome f within the chloroplast.

Main Methods:

  • Crystallization of the globular domain of turnip cytochrome f to enable structural determination.
  • Analysis of protein-protein interactions, specifically between cytochrome f and plastocyanin.
  • Investigation of gene expression and protein synthesis pathways for cytochrome f.

Main Results:

  • The globular domain of turnip cytochrome f has been crystallized, paving the way for detailed 3D structure determination.
  • Interactions involve electrostatic attractions between positively charged regions on cytochrome f and an acidic patch on plastocyanin.
  • Electron transfer occurs via a surface-exposed tyrosine residue on plastocyanin.

Conclusions:

  • Cytochrome f's structure facilitates efficient electron transfer in photosynthesis.
  • The coordinated synthesis of cytochrome f with other cytochrome bf complex subunits ensures proper complex assembly.
  • Understanding cytochrome f structure and function provides insights into thylakoid membrane bioenergetics.