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

Pyruvate Oxidation01:15

Pyruvate Oxidation

168.5K
After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
168.5K
Oxidation Numbers03:14

Oxidation Numbers

42.3K
In redox reactions, the transfer of electrons occurs between reacting species. Electron transfer is described by a hypothetical number called the oxidation number (or oxidation state). It represents the effective charge of an atom or element, which is assigned using a set of rules.
42.3K
Oxidation-Reduction Reactions03:11

Oxidation-Reduction Reactions

75.3K
Oxidation–Reduction Reactions
75.3K
Formation of Complex Ions03:45

Formation of Complex Ions

25.8K
A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
25.8K
Protein Complex Assembly02:41

Protein Complex Assembly

16.7K
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...
16.7K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.9K
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...
2.9K

You might also read

Related Articles

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

Sort by
Same author

From linkage chemistry to active-site engineering: strategic designs and progress in covalent organic frameworks for electrocatalytic hydrogen and oxygen generation.

Materials horizons·2026
Same author

Fundamentals and mechanistic insights for ammonium-ion energy storage: spotlight on metal-organic frameworks.

Materials horizons·2026
Same author

Engineered Hydrogel Incorporated With Doped Carbon Dots Derived From Banana Peel for Pollutant Removal.

Chemistry, an Asian journal·2026
Same author

Synthesis, Characterization, Electronic Structure, and Excitation Dynamics of Dinuclear Copper(I) Complexes with a Naphthyridine Diimine Ligand.

Inorganic chemistry·2025
Same author

Unleashing the Multifunctionality of Carbon Dots for Solar-Driven Interfacial Evaporation: Recent Advances and Diverse Applications.

Chemistry, an Asian journal·2025
Same author

Triazine-Based Porous Organic Polymer Electrocatalysts: Utility and Design Strategy.

Chemistry, an Asian journal·2025

Related Experiment Video

Updated: Jan 26, 2026

Predicting Catalyst Extrudate Breakage Based on the Modulus of Rupture
09:53

Predicting Catalyst Extrudate Breakage Based on the Modulus of Rupture

Published on: May 13, 2018

8.6K

Mannich base Cu(II) complexes as biomimetic oxidative catalyst.

Bidyut Kumar Kundu1, Rishi Ranjan1, Attreyee Mukherjee2

  • 1Discipline of Chemistry, School of Basic Sciences, Indian Institute of Technology Indore, Khandwa Road, Simrol, Indore 453552, India.

Journal of Inorganic Biochemistry
|April 8, 2019
PubMed
Summary
This summary is machine-generated.

New copper complexes mimic galactose oxidase (GOase) and catechol oxidase (COase) enzymes. Complex 1, with a mono-ligand environment, shows superior catalytic activity in mimicking both GOase and COase reactions.

More Related Videos

Preparation of Polyoxometalate-based Photo-responsive Membranes for the Photo-activation of Manganese Oxide Catalysts
05:47

Preparation of Polyoxometalate-based Photo-responsive Membranes for the Photo-activation of Manganese Oxide Catalysts

Published on: August 7, 2018

8.1K
Molten-Salt Synthesis of Complex Metal Oxide Nanoparticles
08:43

Molten-Salt Synthesis of Complex Metal Oxide Nanoparticles

Published on: October 27, 2018

18.8K

Related Experiment Videos

Last Updated: Jan 26, 2026

Predicting Catalyst Extrudate Breakage Based on the Modulus of Rupture
09:53

Predicting Catalyst Extrudate Breakage Based on the Modulus of Rupture

Published on: May 13, 2018

8.6K
Preparation of Polyoxometalate-based Photo-responsive Membranes for the Photo-activation of Manganese Oxide Catalysts
05:47

Preparation of Polyoxometalate-based Photo-responsive Membranes for the Photo-activation of Manganese Oxide Catalysts

Published on: August 7, 2018

8.1K
Molten-Salt Synthesis of Complex Metal Oxide Nanoparticles
08:43

Molten-Salt Synthesis of Complex Metal Oxide Nanoparticles

Published on: October 27, 2018

18.8K

Area of Science:

  • Bioinorganic Chemistry
  • Catalysis
  • Coordination Chemistry

Background:

  • Copper metalloenzymes like Galactose Oxidase (GOase) and catechol oxidase (COase) play crucial roles in biological oxidation reactions.
  • Understanding the structure-activity relationship of copper active sites is key to designing synthetic mimics.
  • Mononuclear copper complexes offer a platform to model the functionalities of these enzymes.

Purpose of the Study:

  • To synthesize and characterize novel mononuclear copper(II) complexes.
  • To investigate the catalytic activities of these complexes in mimicking GOase and COase.
  • To elucidate the mechanistic aspects and identify reactive intermediates during catalysis.

Main Methods:

  • Synthesis of mononuclear copper(II) complexes [CuL(OAc)] (1) and [CuL2] (2).
  • Structural elucidation using X-ray crystallography.
  • Characterization by EPR, GC-MS, HPLC, and ESI-MS.
  • Catalytic studies for GOase and COase mimicking reactions.

Main Results:

  • Complexes 1 and 2 successfully mimicked the catalytic activities of GOase and COase.
  • Complex 1 demonstrated higher catalytic efficiency (kcat, TON) in COase mimicking oxidation of 3,5-DTBC to 3,5-DTBQ compared to complex 2.
  • Benzyl alcohol oxidation to benzaldehyde was significant with complex 1 in the presence of a strong base.
  • Hydrogen peroxide (H2O2) was identified as a byproduct, indicating reactive oxygen species generation.

Conclusions:

  • Mononuclear copper(II) complexes can effectively mimic the catalytic functions of GOase and COase.
  • The coordination environment around the copper center significantly influences catalytic activity, with mono-ligand coordination (Complex 1) being superior.
  • These findings contribute to the development of artificial metalloenzymes for oxidation catalysis.