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

7.2K
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...
7.2K
Oxidation-Reduction Reactions03:11

Oxidation-Reduction Reactions

64.4K
Oxidation–Reduction Reactions
64.4K
Phase I Oxidative Reactions: Overview01:19

Phase I Oxidative Reactions: Overview

246
Phase I biotransformation, or functionalization, is a crucial chemical process that converts drugs and other xenobiotics into more water-soluble forms, facilitating expulsion from the body. It involves oxidative, reductive, and hydrolytic reactions that add or unveil polar functional groups on lipophilic substrates. Key players in phase I reactions are the mixed-function oxidases. Situated in liver cell microsomes, these enzymes predominantly carry out drug metabolism. They require molecular...
246
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.5K
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...
2.5K
Oxidative Cleavage of Alkenes: Ozonolysis01:46

Oxidative Cleavage of Alkenes: Ozonolysis

10.0K
In ozonolysis, ozone is used to cleave a carbon–carbon double bond to form aldehydes and ketones, or carboxylic acids, depending on the work-up.
Ozone is a symmetrical bent molecule stabilized by a resonance structure.
10.0K
Oxygenic Photosynthesis01:26

Oxygenic Photosynthesis

2
Oxygenic photosynthesis is a fundamental process in which light energy is harnessed to drive the oxidation of water, leading to the production of molecular oxygen (O₂), adenosine triphosphate (ATP), and nicotinamide adenine dinucleotide phosphate (NADPH). This process is essential for sustaining aerobic life on Earth and is primarily carried out by cyanobacteria, algae, and plants. The core of oxygenic photosynthesis lies in the thylakoid membranes, where chlorophyll pigments facilitate...
2

You might also read

Related Articles

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

Sort by
Same author

Intramolecular Benzylic Hydroxylation by a {Cu<sub>2</sub>O<sub>2</sub>} Intermediate Leading to an Unusual Trinuclear Copper(II) Species.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Enhancing Cognitive Functions of Older Adults With Software Robot: Longitudinal Exploratory Field Study.

JMIR mHealth and uHealth·2026
Same author

Mechanistic Analysis of Programmed Iteration by Module 5 of the Nocardiosis-Associated Polyketide (NOCAP) Synthase.

Biochemistry·2026
Same author

Chemiluminescent probes for imaging cysteine cathepsin activity.

Bioorganic & medicinal chemistry letters·2025
Same author

Intramolecular Electron Exchange Induced Oxygenation of Aldimine Functions of N,N'-bis(pyridin-2-ylmethylene)Naphthyl-1,5-diimine in Isomeric Diruthenium Frameworks.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Experimental electronic structures of the Fe<sup>IV</sup>=O bond in S=1 heme vs. nonheme sites: Effect of the porphyrin ligand.

Proceedings of the National Academy of Sciences of the United States of America·2025

Related Experiment Video

Updated: Jun 11, 2025

[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

9.2K

Synthetic Copper-(Di)oxygen Complex Generation and Reactivity Relevant to Copper Protein O2-Processing.

Kenneth D Karlin1, Pradip Kumar Hota1, Bohee Kim1

  • 1Department of Chemistry, Johns Hopkins University.

Bulletin of Japan Society of Coordination Chemistry
|October 7, 2024
PubMed
Summary

Synthetic chemists design copper-dioxygen complexes to mimic metalloenzymes. This review highlights ligand systems stabilizing various copper-oxygen species and their reactivity, including electrophilic arene hydroxylation.

Keywords:
copperdioxygenligand-designmetalloenzyme

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

9.1K
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

9.6K

Related Experiment Videos

Last Updated: Jun 11, 2025

[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

9.2K
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

9.1K
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

9.6K

Area of Science:

  • Bioinorganic Chemistry
  • Synthetic Chemistry

Background:

  • Copper-dioxygen complexes are crucial for understanding copper-based metalloenzymes.
  • Designing ligands to mimic enzyme active sites is challenging.

Purpose of the Study:

  • To review ligand systems for stabilizing copper-dioxygen species.
  • To discuss their synthesis, characterization, and reactivity.

Main Methods:

  • Ligand design and synthesis.
  • Spectroscopic characterization of copper-dioxygen species.
  • Reactivity studies, including hydroxylation reactions.

Main Results:

  • Highlighted representative ligand systems stabilizing various copper-dioxygen species (superoxide, peroxide, hydroperoxide).
  • Demonstrated electrophilic arene hydroxylation by a side-on peroxo species via an "NIH shift" mechanism.
  • Discussed thermodynamic-kinetic relationships among different copper-oxygen moieties.

Conclusions:

  • Ligand design is key to stabilizing reactive copper-dioxygen intermediates.
  • Understanding these species advances knowledge of metalloenzyme mechanisms and reactivity.