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...
Colors and Magnetism03:02

Colors and Magnetism

Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

Structural and sequence basis for substrate selection in the cellular trafficking of Fe-S clusters, hemes and glutathione-complexed metals through membrane transporters.

Journal of inorganic biochemistry·2025
Same author

Understanding the Thermodynamics of Magnesium Binding to RNA Structural Motifs.

Life (Basel, Switzerland)·2024
Same author

Influence of the Weak Nuclear Force on Metal-Promoted Autocatalytic Strecker Synthesis of Amino Acids: Formation of a Chiral Pool of Precursors for Prebiotic Peptide and Protein Synthesis.

Life (Basel, Switzerland)·2024
Same author

The long-term health outcomes, pathophysiological mechanisms and multidisciplinary management of long COVID.

Signal transduction and targeted therapy·2023
Same author

Echinacoside regulates PI3K/AKT/HIF-1α/VEGF cross signaling axis in proliferation and apoptosis of breast cancer.

Analytical biochemistry·2023
Same author

8-octyl berberine combats Staphylococcus aureus by preventing peptidoglycan synthesis.

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences·2023

Related Experiment Video

Updated: May 16, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Human ferredoxin-2 displays a unique conformational change.

Wenbin Qi1, Jingwei Li, J A Cowan

  • 1Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.

Dalton Transactions (Cambridge, England : 2003)
|December 5, 2012
PubMed
Summary

Human ferredoxin-2 (hFd2) undergoes a temperature-dependent conformational change, enhancing its interaction with adrenodoxin reductase. This contrasts with human ferredoxin-1 (hFd1), suggesting distinct roles in cellular pathways.

More Related Videos

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Related Experiment Videos

Last Updated: May 16, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Physiology

Background:

  • Human ferredoxin-1 (hFd1) and human ferredoxin-2 (hFd2) are proteins with high sequence similarity.
  • Despite structural similarities, hFd1 and hFd2 participate in different cellular pathways.
  • Understanding the functional differences between hFd1 and hFd2 is crucial for elucidating their distinct roles.

Purpose of the Study:

  • To investigate the structural and functional differences between human ferredoxin-1 and human ferredoxin-2.
  • To explore the impact of temperature on the conformation and activity of hFd2.
  • To compare the interaction of hFd1 and hFd2 with adrenodoxin reductase under physiological conditions.

Main Methods:

  • Comparative analysis of human ferredoxin-1 and human ferredoxin-2 sequences.
  • Temperature-dependent conformational studies of holo hFd2.
  • Enzymatic assays to determine the binding affinity between ferredoxins and adrenodoxin reductase.

Main Results:

  • Holo hFd2 exhibits a unique conformational change upon warming to physiological temperatures.
  • This conformational change in hFd2 leads to an increased affinity for adrenodoxin reductase.
  • No similar temperature-induced conformational change or affinity modulation was observed for hFd1.

Conclusions:

  • The temperature-dependent conformational flexibility of hFd2 is a key factor in its interaction with adrenodoxin reductase.
  • The distinct conformational behavior of hFd1 and hFd2 likely contributes to their specialized functions in separate cellular pathways.
  • These findings provide insights into the differential regulation of electron transport chains involving human ferredoxins.