Related Experiment Video
Updated: May 11, 2026
06:40
Synthesis of a Water-soluble Metal–Organic Complex Array
Published on: October 8, 2016
Artificial metalloenzymes constructed from hierarchically-assembled proteins
Takafumi Ueno1, Hiroyasu Tabe, Yuya Tanaka
1Graduate School of Bioscience and Biotechnology, Tokyo Insitute of Technology, Nagatsuda 4259-B55, Midori-ku, Yokohama 226-8501, Japan. tueno@bio.titech.ac.jp
Chemistry, an Asian Journal
|May 25, 2013
Summary
Artificial metalloenzymes, created by encapsulating metal cofactors in protein scaffolds, show promise in biotechnology. Recent work explores using protein assemblies for advanced artificial enzymes with hierarchical structures.
Area of Science:
- Biophysical Chemistry
- Inorganic Chemistry
- Biotechnology
Background:
- Artificial metalloenzymes are crucial for nanoscience and biotechnology.
- Current methods involve encapsulating metal cofactors within protein scaffolds, yielding active and selective artificial metalloproteins.
- The role of protein assemblies in artificial metalloenzymes remains underexplored despite their significance in natural enzymatic systems.
Purpose of the Study:
- To review recent advancements in artificial metalloenzymes utilizing protein assemblies.
- To highlight the potential of hierarchically assembled proteins for creating novel artificial metalloenzymes.
- To discuss future research directions in this interdisciplinary field.
Main Methods:
- Encapsulation of non-natural metal cofactors within protein scaffolds.
- Functionalization of protein assemblies (e.g., cages, crystals) to host metal complex catalysts.
- Preparation of metal nanoparticles within confined protein environments.
Main Results:
- Demonstration of high activity and selectivity in small artificial metalloproteins.
- Successful application of protein assemblies like cages and crystals as scaffolds for artificial metalloenzymes.
- Creation of confined environments within protein assemblies for catalyst accommodation and nanoparticle synthesis.
Conclusions:
- Artificial metalloenzymes based on hierarchically assembled proteins offer powerful tools for industrial and biological applications.
- Further systematic investigation of protein assemblies is crucial for advancing the field.
- This review provides insights into recent progress and future prospects in artificial metalloenzyme design.
More Related Videos
08:02Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
Published on: August 23, 2018
08:34OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Related Concept Videos
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:13Introduction 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...
02:47Ribozymes
The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes can be...
02:34Enzymes
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 deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
01:07Catalytically 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.
02:51Metal-Ligand Bonds
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...