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

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.3K
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...
8.3K
Enzymes02:34

Enzymes

82.0K
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...
82.0K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

11.1K
Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
11.1K
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

20.2K
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...
20.2K
Enzyme Kinetics01:19

Enzyme Kinetics

97.4K
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...
97.4K

You might also read

Related Articles

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

Sort by
Same author

Oxyalkylation of Alkenes via Triple Radical Sorting.

Journal of the American Chemical Society·2026
Same author

Chemoenzymatic Triazolopyridine Synthesis Enabled by Cryptic Diazo Formation by Vanadium-Dependent Haloperoxidases.

Organic letters·2026
Same author

Biocatalytic Synthesis of Isoxazolines Enabled by Cryptic Nitrile Oxide Formation by a Vanadium-Dependent Chloroperoxidase.

Angewandte Chemie (International ed. in English)·2026
Same author

Chlorination of Amines by a Vanadium-Dependent Chloroperoxidase.

ACS catalysis·2026
Same author

Oxidative Rearrangement of Indoles Enabled by Promiscuous Cryptic Halogenation with Vanadium-Dependent Haloperoxidases.

ACS catalysis·2026
Same author

Chemoenzymatic Diazo Synthesis Enabled by Enzymatic Halide Recycling with Vanadium-Dependent Haloperoxidases.

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: Jul 28, 2025

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

9.1K

Chemoenzymatic Catalysis: Cooperativity Enables Opportunity.

Logan Z Hessefort1, Lauren J Harstad1, Kayla R Merker1

  • 1School of Molecular Sciences, Arizona State University, 551 E University Dr, Tempe, AZ 85281, USA.

Chembiochem : a European Journal of Chemical Biology
|May 30, 2023
PubMed
Summary
This summary is machine-generated.

Enzymes offer selective and sustainable organic synthesis. This review explores their combined use with small molecule catalysts for enhanced chemical reactions and future potential.

Keywords:
biocatalysischemoenzymaticcooperativeelectrocatalysisorganocatalysis

More Related Videos

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

Published on: January 17, 2020

7.3K
Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

17.4K

Related Experiment Videos

Last Updated: Jul 28, 2025

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

9.1K
Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

Published on: January 17, 2020

7.3K
Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

17.4K

Area of Science:

  • Synthetic organic chemistry
  • Biocatalysis
  • Chemoenzymatic catalysis

Background:

  • Enzymes are increasingly used in synthetic sequences for selective, efficient, and sustainable chemical synthesis.
  • Cooperative catalysis combining enzymes with small molecule catalysts is a growing area of interest.

Purpose of the Study:

  • To review notable achievements in cooperative chemoenzymatic catalysis.
  • To provide a perspective on the future directions of this field.

Main Methods:

  • Literature review of cooperative chemoenzymatic catalysis.
  • Analysis of successful integration of enzymes and small molecule catalysts.

Main Results:

  • Enzymatic catalysis provides a powerful tool for generating molecular complexity.
  • Cooperative chemoenzymatic catalysis enhances synthetic efficiency and selectivity.
  • Numerous academic and industrial applications demonstrate the utility of this approach.

Conclusions:

  • Cooperative chemoenzymatic catalysis represents a significant advancement in organic synthesis.
  • This approach offers a sustainable and efficient route to complex molecules.
  • Future research holds promise for expanding the scope and applications of chemoenzymatic catalysis.