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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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...
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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...
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Catalysis02:50

Catalysis

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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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Induced-fit Model01:13

Induced-fit Model

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Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
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Enzymes02:34

Enzymes

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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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.
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Related Experiment Video

Updated: Jul 17, 2025

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
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Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes

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How Flexibility Can Enhance Catalysis.

Olivier Rivoire1

  • 1Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, and Gulliver, CNRS, ESPCI, Université Paris Sciences et Lettres, 75005 Paris, France.

Physical Review Letters
|September 8, 2023
PubMed
Summary

Enzymes overcome limitations in catalysis through conformational changes. This theoretical model shows how substrate binding can induce these changes, enabling barrier-free catalysis and improving artificial catalyst design.

Area of Science:

  • Biochemistry
  • Theoretical Chemistry
  • Enzyme Kinetics

Background:

  • Enzyme conformational changes are widely observed but their catalytic role remains debated.
  • Rigid catalysts exhibit inherent limitations compared to biological enzymes.
  • Previous theories suggest protein-specific features contribute to enzyme efficiency.

Purpose of the Study:

  • To present a theoretical model explaining how conformational changes enhance catalysis.
  • To illustrate the limitations of rigid catalysts.
  • To propose a mechanism for achieving barrier-free catalysis.

Main Methods:

  • Development of a minimal theoretical model.
  • Analysis of substrate-induced conformational changes.
  • Comparison with existing catalytic theories and protein features.

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Applying Dynamic Strain on Thin Oxide Films Immobilized on a Pseudoelastic Nickel-Titanium Alloy
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Applying Dynamic Strain on Thin Oxide Films Immobilized on a Pseudoelastic Nickel-Titanium Alloy

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Related Experiment Videos

Last Updated: Jul 17, 2025

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
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Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Applying Dynamic Strain on Thin Oxide Films Immobilized on a Pseudoelastic Nickel-Titanium Alloy
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Applying Dynamic Strain on Thin Oxide Films Immobilized on a Pseudoelastic Nickel-Titanium Alloy

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Main Results:

  • The model demonstrates how conformational changes overcome rigid catalyst limitations.
  • Substrate binding can trigger a 'discriminative switch' enabling enhanced catalysis.
  • The principle explains the superiority of enzymes over other catalysts.

Conclusions:

  • Conformational flexibility is crucial for enzymes to achieve high catalytic efficiency.
  • The proposed mechanism offers insights into barrier-free catalysis.
  • The model provides a framework for designing improved artificial catalysts.