Related Experiment Video
Updated: May 11, 2026
09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Bimolecular catalysis and turnover from a macromolecular host system
Adam Ellis1, David Gooch, Lance J Twyman
1Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield S3 7HF, UK.
The Journal of Organic Chemistry
|May 14, 2013
Summary
Researchers developed a novel globular macromolecule acting as a bimolecular catalyst. This synthetic catalyst significantly accelerates reactions by bringing reactants together, showing high turnover rates and overcoming product inhibition common in other catalysts.
Area of Science:
- Supramolecular Chemistry
- Catalysis
- Macromolecular Science
Background:
- Synthetic catalysts often suffer from product inhibition, limiting their efficiency.
- Controlling reactant proximity is key to enhancing bimolecular reaction rates.
- Macromolecular hosts offer unique environments for catalytic applications.
Purpose of the Study:
- To synthesize a globular macromolecule capable of bimolecular catalysis.
- To investigate the catalytic activity and mechanism of the synthesized macromolecule.
- To overcome product inhibition observed in conventional synthetic catalysts.
Main Methods:
- Synthesis of a globular macromolecule featuring zinc-metalated porphyrin units.
- Characterization of the macromolecule's binding capabilities for reactants.
- Kinetic studies to determine reaction rates and catalytic efficiency.
- Analysis of product displacement and turnover mechanisms.
Main Results:
- The macromolecule successfully binds two reactants, increasing local concentration.
- A maximum 300-fold increase in reaction rate was observed.
- The system demonstrated efficient turnover, with product displacement by reactants.
- The macromolecule's dynamic flexibility was identified as crucial for catalysis and overcoming inhibition.
Conclusions:
- A novel globular macromolecule functions as an efficient bimolecular catalyst.
- The catalyst design overcomes product inhibition through dynamic host-guest interactions.
- This work presents a new strategy for designing highly active and recyclable synthetic catalysts.
Related Concept Videos
01:13Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
01:13Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
01:28ATP and Macromolecule Synthesis
Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
Conversion of...
Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
Conversion of...
01:19Turnover 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...
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion. The...
01:22Heterogeneous 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...
02:50Catalysis
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.