Supramolecular Enzyme Mimics

Y. Okamoto; T. R. Ward

doi:10.1016/B978-0-12-409547-2.12551-X

Supramolecular Enzyme Mimics

Y. Okamoto, T. R. Ward

Research output: Chapter in Book/Report/Conference proceeding › Chapter

7 Citations (Scopus)

Abstract

Artificial metalloenzymes result from the incorporation of an organometallic moiety within a macromolecule. In this article, we review the field of artificial metalloenzymes. These are classified according to the host that accommodates the organometallic cofactor: cyclodextrins ("Cyclodextrin-Based Artificial Enzymes" section), ligands bearing a substrate recognition motif ("Artificial Enzymes With Ligands Bearing Substrate Recognition Motifs" section), supramolecular cages ("Cage Molecules as Artificial Enzymes" section), nucleic acids ("DNA-Based Artificial Metalloenzymes" section), and proteins ("Protein-Based Artificial Enzymes" section). Both dative and supramolecular anchoring strategies are reviewed.

Original language	English
Title of host publication	Bioinspired and Biomimetic Supramolecular Chemistry
Publisher	Elsevier Inc.
Pages	459-510
Number of pages	52
Volume	4
ISBN (Electronic)	9780128031988
ISBN (Print)	9780128031995
DOIs	https://doi.org/10.1016/B978-0-12-409547-2.12551-X
Publication status	Published - 2017 Jun 22
Externally published	Yes

Keywords

Artificial metalloenzyme
Cage molecule
Catalysis
Cyclodextrin
Dative anchoring
Double-stranded DNA
G-quadruplex
Hydrogen bonding
Molecular recognition
Protein
Reaction compartment
Supramolecular anchoring

ASJC Scopus subject areas

Chemistry(all)

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10.1016/B978-0-12-409547-2.12551-X

Cite this

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abstract = "Artificial metalloenzymes result from the incorporation of an organometallic moiety within a macromolecule. In this article, we review the field of artificial metalloenzymes. These are classified according to the host that accommodates the organometallic cofactor: cyclodextrins ({"}Cyclodextrin-Based Artificial Enzymes{"} section), ligands bearing a substrate recognition motif ({"}Artificial Enzymes With Ligands Bearing Substrate Recognition Motifs{"} section), supramolecular cages ({"}Cage Molecules as Artificial Enzymes{"} section), nucleic acids ({"}DNA-Based Artificial Metalloenzymes{"} section), and proteins ({"}Protein-Based Artificial Enzymes{"} section). Both dative and supramolecular anchoring strategies are reviewed.",

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AU - Ward, T. R.

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AB - Artificial metalloenzymes result from the incorporation of an organometallic moiety within a macromolecule. In this article, we review the field of artificial metalloenzymes. These are classified according to the host that accommodates the organometallic cofactor: cyclodextrins ("Cyclodextrin-Based Artificial Enzymes" section), ligands bearing a substrate recognition motif ("Artificial Enzymes With Ligands Bearing Substrate Recognition Motifs" section), supramolecular cages ("Cage Molecules as Artificial Enzymes" section), nucleic acids ("DNA-Based Artificial Metalloenzymes" section), and proteins ("Protein-Based Artificial Enzymes" section). Both dative and supramolecular anchoring strategies are reviewed.

KW - Artificial metalloenzyme

KW - Cage molecule

KW - Catalysis

KW - Cyclodextrin

KW - Dative anchoring

KW - Double-stranded DNA

KW - G-quadruplex

KW - Hydrogen bonding

KW - Molecular recognition

KW - Protein

KW - Reaction compartment

KW - Supramolecular anchoring

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AN - SCOPUS:85045793469

SN - 9780128031995

VL - 4

SP - 459

EP - 510

BT - Bioinspired and Biomimetic Supramolecular Chemistry

PB - Elsevier Inc.

ER -

Supramolecular Enzyme Mimics

Abstract

Keywords

ASJC Scopus subject areas

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