Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis

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 Catalysis

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 Enzyme Kinetics

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...

Enzymes

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...

Enzyme Kinetics

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

Catalytically Perfect Enzymes

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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Correction to "Monooxygenase Activity of Indoleamine 2,3-Dioxygenase".

Journal of the American Chemical Society·2026

Same author

Decarboxylation via a Higher Electronic Excited State Drives LSSmOrange Photoconversion.

ACS physical chemistry Au·2026

Same author

Free energy simulations on a biomimetic glucose receptor: understanding the selectivity of GluHUT.

Chemical science·2026

Same author

Autonomic indicators of self-transcendence: insights from the numadelic VR paradigm.

Neuroscience of consciousness·2026

Same author

Hydrogen-Bonding Changes Cause Differences in Imipenem Breakdown Activity in OXA-48 Variants.

Journal of chemical information and modeling·2026

Same author

Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.

Protein science : a publication of the Protein Society·2026

Search research articles

Related Experiment Video

Updated: May 24, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Taking Ockham's razor to enzyme dynamics and catalysis.

David R Glowacki¹, Jeremy N Harvey, Adrian J Mulholland

¹Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, UK. David.R.Glowacki@bristol.ac.uk

Nature Chemistry

|February 23, 2012

Summary

Protein dynamics influence enzyme catalysis, especially in reactions with quantum tunneling. A transition-state theory model, including multiple protein conformations, successfully explains experimental enzyme kinetics.

More Related Videos

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Related Experiment Videos

Last Updated: May 24, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Area of Science:

Biochemistry
Chemical Kinetics
Quantum Mechanics

Background:

The role of protein dynamics in enzyme catalysis is debated.
Quantum tunneling in enzyme reactions complicates kinetic isotope effects and challenges standard rate theories like transition-state theory.

Purpose of the Study:

To re-evaluate transition-state theory for enzyme reactivity.
To explain complex experimental observations in enzyme catalysis.

Main Methods:

Drawing parallels with gas-phase and solution-phase chemical kinetics.
Applying a modified transition-state theory framework incorporating multiple conformations.

Main Results:

Experimental kinetic isotope effects with complex temperature dependencies can be explained.
A transition-state theory model with multiple conformations accurately reproduces enzyme activity data.

Conclusions:

Transition-state theory, when extended to include protein conformational flexibility, provides a viable framework for understanding enzyme catalysis.
Protein dynamics, specifically conformational heterogeneity, are crucial for explaining enzyme reactivity, particularly in reactions involving quantum tunneling.