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

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...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

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...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.

You might also read

Related Articles

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

Sort by
Same author

Grafted Coiled-Coil Peptides as Multivalent Scaffolds for Protein Recognition.

ACS chemical biology·2025
Same author

Differential sensing with arrays of de novo designed peptide assemblies.

Nature communications·2023
Same author

De novo designed peptides for cellular delivery and subcellular localisation.

Nature chemical biology·2022
Same author

Coiled coils 9-to-5: rational <i>de novo</i> design of α-helical barrels with tunable oligomeric states.

Chemical science·2021
Same author

How Coiled-Coil Assemblies Accommodate Multiple Aromatic Residues.

Biomacromolecules·2021
Same author

Structural resolution of switchable states of a de novo peptide assembly.

Nature communications·2021

Related Experiment Video

Updated: Jul 5, 2026

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Artificial metalloenzymes in complex biological environments.

Guto G Rhys1

  • 1School of Chemistry, Cardiff University, Cardiff, UK. rhysg3@cardiff.ac.uk.

Nature Chemical Biology
|July 3, 2026
PubMed
Summary

This study explores robust, biocompatible artificial metalloenzymes (ArMs) for cellular applications. It details strategies for ArMs to function within cells, on surfaces, or in lysates, addressing challenges for improved performance.

More Related Videos

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
09:51

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Related Experiment Videos

Last Updated: Jul 5, 2026

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
09:51

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Area of Science:

  • Biochemistry
  • Bioengineering
  • Synthetic Biology

Background:

  • Artificial metalloenzymes (ArMs) combine protein scaffolds with metal cofactors to catalyze novel reactions.
  • ArMs show potential in fine-chemical synthesis, cellular control, and therapeutics.
  • Challenges include cofactor instability and cellular stress in biological settings.

Purpose of the Study:

  • To review recent strategies for developing robust and biocompatible ArMs.
  • To evaluate ArM functionality in cell lysates, on cell surfaces, and intracellularly.
  • To discuss challenges and opportunities in ArM development and application.

Main Methods:

  • Literature review of recent advancements in artificial metalloenzyme design and application.
  • Analysis of strategies for enhancing ArM robustness and biocompatibility.
  • Comparative assessment of ArM performance in different cellular environments (lysates, surface, intracellular).

Main Results:

  • Identified key strategies for creating ArMs that tolerate complex biological environments.
  • Described the advantages and disadvantages of using ArMs in cell lysates, on cell surfaces, and intracellularly.
  • Highlighted the need for improved construction methods and catalytic efficiency.

Conclusions:

  • Robust, biocompatible ArMs can be engineered for diverse cellular applications.
  • Further research is needed to overcome challenges in ArM construction, performance, and reaction scope.
  • ArMs offer significant opportunities for biocatalysis and biotechnology.