Related Experiment Video

Updated: Jan 21, 2026

Facile Synthesis of Worm-like Micelles by Visible Light Mediated Dispersion Polymerization Using Photoredox Catalyst
07:39

Facile Synthesis of Worm-like Micelles by Visible Light Mediated Dispersion Polymerization Using Photoredox Catalyst

Published on: June 8, 2016

9.9K

Improved Catalytic Performance of Au/α-Fe2O3-Like-Worm Catalyst for Low Temperature CO Oxidation

Qiuwan Han1, Dongyang Zhang1, Jiuli Guo1

  • 1Key Laboratory of Advanced Energy Material Chemistry (MOE), TKL of Metal and Molecule Based Material Chemistry, Department of Chemistry, Nankai University, Tianjin 300071, China.

Nanomaterials (Basel, Switzerland)
|August 7, 2019
PubMed

Keywords:
Au/α-Fe2O3CO oxidationworm-like

More Related Videos

Temperature-programmed Deoxygenation of Acetic Acid on Molybdenum Carbide Catalysts08:15

Temperature-programmed Deoxygenation of Acetic Acid on Molybdenum Carbide Catalysts

Published on: February 7, 2017

11.8K
Synthesis and Catalytic Performance of Gold Intercalated in the Walls of Mesoporous Silica11:02

Synthesis and Catalytic Performance of Gold Intercalated in the Walls of Mesoporous Silica

Published on: July 9, 2015

10.6K

Related Concept Videos

Oxidation Numbers03:14

Oxidation Numbers

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.
42.2K
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....
20.3K
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.
 
Most enzymes...
4.9K
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
14.1K
Pyruvate Oxidation01:15

Pyruvate Oxidation

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+...
168.4K
Oxidation-Reduction Reactions03:11

Oxidation-Reduction Reactions

Oxidation–Reduction Reactions
75.2K