Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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.
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...
Enzyme Kinetics01:19

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...
Introduction to Enzyme Kinetics01:19

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...

You might also read

Related Articles

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

Sort by
Same author

Macroscopic Convective Fluid Flows Arising From Binding of Ions and Small Molecules to Proteins.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Emergent Nonlinearity in Active Molecular Chemotaxis.

ACS nano·2026
Same author

Chemotaxis of ATPase-Powered Nanoparticles up Extra- and Intracellular ATP Gradients.

Nano letters·2026
Same author

A Monolithic Artificial Leaf for Solar Methanol Production from CO<sub>2</sub> and H<sub>2</sub>O.

Journal of the American Chemical Society·2026
Same author

Silver Oxide Nanoparticles as Solid-State Hydroxide Ion Conductors for Watt-Scale Anion Exchange Membrane Fuel Cells.

ACS energy letters·2026
Same author

Nonequilibrium surfactant partitioning into microdroplets generates local phase inversion conditions and interfacial instability.

Soft matter·2026
Same journal

Linker Engineering toward NIR-II Metal-Organic Framework with Maximal Emission beyond 1000 nm for Inflammatory Bowel Disease Imaging.

Journal of the American Chemical Society·2026
Same journal

Observing Kinetic Selectivity in Anthracene Photodimerization through Selective Quenching by Excited States of Proximate Rare Earth Cations.

Journal of the American Chemical Society·2026
Same journal

Sequence-Dependent Folding of Recognition-Encoded Melamine Oligomers.

Journal of the American Chemical Society·2026
Same journal

Large Thermo- and Mechanosalient Actuation via Cooperative Twist Elasticity-Induced Packing Motif Conversion.

Journal of the American Chemical Society·2026
Same journal

Discovery and Biosynthesis of Lanthipeptides Featuring an Azepinoindole Scaffold by Radical <i>S</i>-Adenosylmethionine Enzyme-Catalyzed C-C Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Enantiopurity-Controlled Magnetism in a Two-Dimensional Organic-Inorganic Material.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Jun 16, 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

Substrate catalysis enhances single-enzyme diffusion.

Hari S Muddana1, Samudra Sengupta, Thomas E Mallouk

  • 1Departments of Bioengineering, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

Journal of the American Chemical Society
|January 30, 2010
PubMed
Summary
This summary is machine-generated.

Single urease enzyme molecules show increased diffusion with urea, driven by a 12 pN self-electrophoretic force per reaction. This finding advances understanding of biological force generation and enzyme nanomotors.

More Related Videos

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

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

Published on: August 19, 2013

Related Experiment Videos

Last Updated: Jun 16, 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

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

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

Published on: August 19, 2013

Area of Science:

  • Biophysics
  • Enzymology
  • Nanotechnology

Background:

  • Enzyme catalysis can generate forces at the molecular level.
  • Understanding enzyme-driven forces is crucial for nanomotor development.

Purpose of the Study:

  • To quantify the force generated by single urease enzyme molecules during urea catalysis.
  • To investigate the mechanism behind enzyme-induced molecular diffusion changes.

Main Methods:

  • Fluorescence Correlation Spectroscopy (FCS) to measure single-molecule diffusion.
  • Enzyme inhibition studies using pyrocatechol.
  • pH measurements using SNARF-1.
  • Brownian dynamics simulations to calculate force.

Main Results:

  • Urease diffusion increased by 16-28% in the presence of urea (0.001-1 M).
  • This increase was dependent on urea catalysis and significantly reduced by enzyme inhibition.
  • Local pH changes were insufficient to explain the observed diffusion increase.
  • A self-electrophoretic force of 12 pN per reaction turnover was calculated.

Conclusions:

  • Single urease molecules generate a measurable force during catalysis.
  • Self-electrophoresis is the most plausible mechanism for this force generation.
  • This study provides a foundation for developing enzyme-driven nanomotors.