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

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

5.8K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
5.8K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

16.5K
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...
16.5K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.5K
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...
8.5K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.4K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.4K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.7K
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...
2.7K
Electron Transport Chain Components01:29

Electron Transport Chain Components

506
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...
506

You might also read

Related Articles

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

Sort by
Same author

The two alternative NADH:quinone oxidoreductases from <i>Staphylococcus aureus</i>: two players with different molecular and cellular roles.

Microbiology spectrum·2024
Same author

The monotopic quinone reductases from Staphylococcus aureus.

Biochimica et biophysica acta. Bioenergetics·2024
Same author

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

Biochimica et biophysica acta. Bioenergetics·2023
Same author

The protein family of pyruvate:quinone oxidoreductases: Amino acid sequence conservation and taxonomic distribution.

Biochimica et biophysica acta. Bioenergetics·2023
Same author

Unveiling the membrane bound dihydroorotate: Quinone oxidoreductase from Staphylococcus aureus.

Biochimica et biophysica acta. Bioenergetics·2022
Same author

Modularity of membrane-bound charge-translocating protein complexes.

Biochemical Society transactions·2021

Related Experiment Video

Updated: Nov 7, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.4K

The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes.

Filipa Calisto1,2, Manuela M Pereira1,2

  • 1Instituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.

Frontiers in Chemistry
|April 30, 2021
PubMed
Summary

NrfD-like subunits are integral membrane proteins essential for energy transduction in microbial enzymes. These subunits, found in diverse complexes, may function as ion-pumping modules, impacting cellular energy processes.

Keywords:
CISM familyNrfD-likeenergy transductionion translocationmembrane proteinquinine/quinol binding site

More Related Videos

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.6K
Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission F&#246;rster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

629

Related Experiment Videos

Last Updated: Nov 7, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.4K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.6K
Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission F&#246;rster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

629

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Integral membrane proteins link peripheral enzyme subunits to the membrane.
  • NrfD-like subunits interact with quinones but lack redox cofactors.
  • Periplasmic nitrite reductase (NrfABCD) first identified this subunit type, naming the family NrfD.

Purpose of the Study:

  • To analyze the primary structure of NrfD-like subunits.
  • To build structural models of NrfD-like subunits.
  • To investigate the potential function of NrfD-like subunits in energy transduction.

Main Methods:

  • Sequence analysis of NrfD homologs across diverse microbial enzymes.
  • Primary structural analysis of NrfD-like subunits.
  • Computational structural modeling of NrfD-like subunits.

Main Results:

  • NrfD homologs are present in numerous enzymes including PsrABC, ACIII, DmsABC, and others.
  • Structural models reveal NrfD-like subunits consist of two four-helix bundle repeats.
  • These subunits possess potential ion-conducting pathways and quinone/quinol binding sites.

Conclusions:

  • NrfD-like subunits are conserved across various energy-transducing enzymes.
  • They likely function as ion-pumping modules.
  • Their role in ion transport is crucial for the energy transduction capabilities of these enzyme complexes.