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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion. The...
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
Heterogeneous Catalysis01:22

Heterogeneous Catalysis

Heterogeneous catalysis involves a catalyst in a different phase from the reactants. It is a process where the catalyst and the reactants are in distinct phases, typically solid and gas or liquid.Most heterogeneous catalysts are metals, metal oxides, or acids. The list includes transition metals like iron (Fe), cobalt (Co), nickel (Ni), palladium (Pd), platinum (Pt), chromium (Cr), manganese (Mn), tungsten (W), silver (Ag), and copper (Cu). These metals possess partially vacant d orbitals that...
Catalysis01:27

Catalysis

Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...
Catalysis02:50

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.

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Related Experiment Video

Updated: Jun 10, 2026

An In Vitro Enzymatic Assay to Measure Transcription Inhibition by Gallium(III) and H3 5,10,15-tris(pentafluorophenyl)corroles
09:00

An In Vitro Enzymatic Assay to Measure Transcription Inhibition by Gallium(III) and H3 5,10,15-tris(pentafluorophenyl)corroles

Published on: March 18, 2015

Highly efficient catalase activity of metallocorroles.

Atif Mahammed1, Zeev Gross

  • 1Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 32000, Israel.

Chemical Communications (Cambridge, England)
|August 24, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces an iron(iii) corrole complex that effectively breaks down hydrogen peroxide. This compound demonstrates superior catalase-like activity compared to other synthetic catalysts.

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An In Vitro Enzymatic Assay to Measure Transcription Inhibition by Gallium(III) and H3 5,10,15-tris(pentafluorophenyl)corroles
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Area of Science:

  • Biomimetic chemistry
  • Catalysis
  • Materials science

Background:

  • Hydrogen peroxide (H2O2) is a reactive oxygen species implicated in various biological processes and diseases.
  • Developing efficient catalysts for H2O2 decomposition is crucial for therapeutic and diagnostic applications.
  • Synthetic catalysts mimicking natural enzymes like catalase offer potential solutions.

Purpose of the Study:

  • To synthesize and characterize a novel iron(iii) corrole complex.
  • To investigate the catalytic activity of this complex in hydrogen peroxide decomposition.
  • To evaluate its potential for protein-mediated cellular uptake and therapeutic applications.

Main Methods:

  • Synthesis and characterization of the iron(iii) corrole complex.
  • Kinetic studies to determine the catalytic efficiency (kcat, turnover frequency) for H2O2 decomposition.
  • Assessment of protein binding and protein-mediated cellular uptake.

Main Results:

  • The iron(iii) corrole complex exhibits strong binding to proteins.
  • The complex undergoes efficient protein-mediated cellular uptake.
  • It catalyzes H2O2 decomposition with a high rate constant (kcat = 6400 M(-1) s(-1)) and turnover frequency (>120 s(-1)).
  • This activity surpasses previously reported synthetic catalase mimics.

Conclusions:

  • The developed iron(iii) corrole complex is a highly efficient biomimetic catalyst for hydrogen peroxide decomposition.
  • Its ability to bind proteins and undergo cellular uptake suggests potential therapeutic applications.
  • This research opens avenues for novel drug development targeting oxidative stress.