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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction 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...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction 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...
Enzymes02:34

Enzymes

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.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Introduction To Enzymes01:22

Introduction To Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Enzymes and Activation Energy01:13

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...

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Related Experiment Video

Updated: May 24, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Good vibrations in enzyme-catalysed reactions.

Sam Hay1, Nigel S Scrutton

  • 1Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK. sam.hay@manchester.ac.uk

Nature Chemistry
|February 23, 2012
PubMed
Summary

Fast enzyme motions may lower reaction energy barriers, aiding hydrogen transfer. Direct evidence for these

Area of Science:

  • Biochemistry and Enzymology
  • Physical Chemistry
  • Computational Chemistry

Background:

  • Enzyme-catalyzed reactions are crucial in biological systems.
  • The role of fast molecular motions (femtosecond-picosecond timescales) in enzymatic reactions is an emerging area of interest.
  • Indirect evidence, such as kinetic isotope effects and simulations, suggests these motions might influence reaction pathways.

Purpose of the Study:

  • To explore the hypothesis that fast 'promoting' or 'compressive' motions can reduce energy barriers in enzymatic reactions.
  • To investigate the potential contribution of these motions to quantum mechanical and classical nuclear-transfer chemistry, particularly hydrogen transfer.
  • To discuss the current state of direct experimental evidence for compressive motions in enzymes.

Main Methods:

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Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation
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Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation

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Last Updated: May 24, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation

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  • Review and discussion of indirect experimental evidence (e.g., anomalous temperature dependence of kinetic isotope effects).
  • Analysis of insights gained from computational simulations.
  • Exploration of theoretical concepts linking fast motions to enzymatic catalysis.

Main Results:

  • Indirect experimental data and computational simulations suggest that fast enzyme motions can influence reaction dynamics.
  • These motions, termed 'promoting' or 'compressive', are hypothesized to lower activation energy barriers.
  • Direct atomic-level demonstration and understanding of these motions remain a challenge.

Conclusions:

  • Fast enzyme motions, specifically compressive motions, show potential for facilitating hydrogen-transfer reactions by lowering energy barriers.
  • While indirect evidence is supportive, direct experimental validation and detailed structural understanding are still needed.
  • Further research combining experimental and computational approaches is essential to fully elucidate the role of these motions in enzyme catalysis.