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

9.0K
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...
9.0K
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

4.5K
In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
4.5K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.9K
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...
2.9K
The Electron Transport Chain01:30

The Electron Transport Chain

19.6K
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...
19.6K
Radical Autoxidation01:20

Radical Autoxidation

3.1K
The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
3.1K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

18.4K
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...
18.4K

You might also read

Related Articles

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

Sort by
Same author

On-demand peptide therapeutics for multi-year space exploration: analysis of clinical and operational relevance and recombinant production feasibility.

NPJ microgravity·2026
Same author

The ultrarapid delayed rectifier potassium current has important functional role in the repolarization reserve of canine and human ventricular muscle.

The Journal of physiology·2026
Same author

Mimicking LPMO Active Sites with Synthetic copper(II) Complexes: Exploring the Minimal Requirements.

Inorganic chemistry·2026
Same author

Organometallic Complexes with an Indolo[2,3-<i>c</i>]Quinoline-Derived Ligand: From Structural Features and Solution Speciation to Nanoformulation for Enhanced Therapeutic Potential.

Inorganic chemistry·2026
Same author

Do small-conductance Ca<sup>2+</sup>-activated K<sup>+</sup>-channels contribute to ventricular repolarization in human heart failure?

American journal of physiology. Heart and circulatory physiology·2026
Same author

The impact of plyometric and small-sided games training on physical performance in adolescent female handball players.

Frontiers in sports and active living·2026

Related Experiment Video

Updated: Jan 14, 2026

[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst
09:12

[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst

Published on: May 21, 2019

9.8K

Chromone-Based Antioxidant Copper(II) Complex with High Superoxide Dismutase Activity.

Dóra Vargáné Szalóki1, Mira Szabó2, Dóra Bonczidai-Kelemen2

  • 1HUN-REN-DE Mechanisms of Complex Homogeneous and Heterogeneous Chemical Reactions Research Group, University of Debrecen, Egyetem tér 1., H-4032 Debrecen, Hungary.

Inorganic Chemistry
|October 23, 2025
PubMed
Summary

Researchers developed a novel copper(II) complex with a chromone-based ligand, ChroHis, demonstrating excellent antioxidant and superoxide dismutase (SOD) activity. This non-toxic complex shows promise for treating diseases linked to high superoxide levels.

More Related Videos

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.7K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.0K

Related Experiment Videos

Last Updated: Jan 14, 2026

[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst
09:12

[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst

Published on: May 21, 2019

9.8K
Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.7K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.0K

Area of Science:

  • Medicinal Chemistry
  • Biochemistry
  • Materials Science

Background:

  • Transition metal complexes can mimic superoxide dismutase (SOD) enzymes for antioxidant therapy.
  • Chromone-based compounds show antioxidant potential but suffer from poor solubility and metal binding.
  • Developing novel ligands is crucial for enhancing the efficacy of metal-based antioxidants.

Purpose of the Study:

  • To synthesize and characterize a novel chromone-based ligand, ChroHis, with improved properties.
  • To investigate the complexation of ChroHis with copper(II) and evaluate its antioxidant capabilities.
  • To assess the therapeutic potential of the copper(II)/ChroHis complex for diseases involving elevated superoxide levels.

Main Methods:

  • Synthesis of ChroHis ligand and its copper(II) complexes.
  • Solution equilibrium studies and spectroscopic analyses (e.g., UV-Vis, EPR).
  • Electrochemical studies (cyclic voltammetry) and enzymatic assays (SOD activity tests).
  • In vitro cell viability and proliferation assays.

Main Results:

  • ChroHis exhibits enhanced water solubility and forms stable dimeric copper(II) complexes.
  • The copper(II)/ChroHis complex displays optimal redox potentials for superoxide dismutation.
  • Excellent SOD activity and significant antioxidant efficacy were confirmed through kinetic and biochemical assays.
  • The complex demonstrated negligible cytotoxicity in vitro, indicating a wide safety margin.

Conclusions:

  • The novel ChroHis ligand facilitates the formation of stable, highly active copper(II) complexes.
  • The Cu(II)/ChroHis complex possesses potent SOD activity and favorable thermodynamic stability.
  • Its non-toxic profile and high efficacy suggest strong potential for antioxidant therapeutic applications.