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...
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...
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

You might also read

Related Articles

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

Sort by
Same author

A multilayered cell envelope of a member of the Chloroflexota offers an anchoring platform for the archaellum.

Frontiers in microbiology·2026
Same author

The Interstitial Collagenases MMP13 and MMP14 Are Dispensable for the Early Onset of Skin Morphogenesis but Modulate Endochondral Ossification.

The American journal of pathology·2026
Same author

A ULK1-MTFR1L feedback loop links mitochondrial fission, mitophagy and apoptosis.

Journal of cell science·2026
Same author

Rejuvenation of the Aged Cerebrovascular System via Protein Corona-Guided Fusogenic Liposome Delivery.

bioRxiv : the preprint server for biology·2026
Same author

Proteomic characterization of intrahepatic cholangiocarcinoma identifies risk-stratifying subgroups and EIF4A1 as a therapeutic target.

Nature communications·2026
Same author

Controlled Delivery and Light-Induced Release of Magic Spot Nucleotides in Escherichia coli.

Angewandte Chemie (International ed. in English)·2026

Related Experiment Video

Updated: Jul 16, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Distinct Assembly Complexes facilitate cbb3-type Cytochrome Oxidase Maturation.

Kaiwei Shen1, Yavuz Öztürk2, Jorge Jimenez-Niebla3

  • 1Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg 79104 Freiburg, Germany; Faculty of Biology, Albert-Ludwigs-University Freiburg 79104 Freiburg, Germany.

Journal of Molecular Biology
|July 14, 2026
PubMed
Summary

Bacterial cytochrome oxidase (Cox) assembly involves large, stable protein complexes, challenging previous assumptions. These complexes coordinate cofactor insertion for cbb3-Cox maturation in R. capsulatus.

Keywords:
Rhodobacter capsulatuscopper homeostasiscytochrome oxidasecytochromesprotein assembly

More Related Videos

Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples
05:45

Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples

Published on: May 3, 2024

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: Jul 16, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples
05:45

Isolation of Mitochondria for Mitochondrial Supercomplex Analysis from Small Tissue and Cell Culture Samples

Published on: May 3, 2024

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:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Cytochrome oxidase (Cox) assembly requires precise coordination of subunit association and cofactor insertion.
  • Mitochondrial Cox assembly utilizes large machineries, while bacterial assembly was thought to involve transient interactions.

Purpose of the Study:

  • To investigate the mechanisms of cbb3-type Cytochrome oxidase assembly in the α-proteobacterium R. capsulatus.
  • To identify the protein complexes involved in bacterial Cox maturation.

Main Methods:

  • Identification and characterization of stable protein complexes during cbb3-Cox assembly.
  • Analysis of cofactor insertion pathways mediated by these complexes.

Main Results:

  • Three stable assembly complexes (500, 390, and 150 kDa) were identified.
  • These complexes facilitate stepwise heme and copper insertion.
  • A copper insertion module involving CcoG, CcoI, SenC, and CcoS was characterized.

Conclusions:

  • Large multi-protein assembly machineries, similar to those in mitochondria, are essential for bacterial cbb3-Cox maturation.
  • Bacterial Cox assembly is more complex than previously assumed, involving stable intermediate complexes.
  • Copper loading onto CcoG and CcoI regulates the formation and stability of these assembly complexes.