Solids Go Bio: Inorganic Nanoparticles as Enzyme Mimics

A longstanding goal of biomimetic chemistry is the design and synthesis of functional enzyme mimics. The past three decades have seen a wide variety of materials, including metal complexes, polymers and other biomolecules, that mimic the structures and functions of naturally occurring enzymes. Among...

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Bibliographic Details
Published in:European journal of inorganic chemistry Vol. 2016; no. 13-14; pp. 1906 - 1915
Main Authors: Ragg, Ruben, Tahir, Muhammad N., Tremel, Wolfgang
Format: Journal Article
Language:English
Published: Weinheim WILEY-VCH Verlag 01.05.2016
WILEY‐VCH Verlag
Wiley Subscription Services, Inc
Subjects:
Biocatalysis
Biomimetics
Enzyme mimics
Enzymes
Metalloenzymes
Nanomaterials
Nanoparticles
Oxidase
Oxidoreductases
Peroxidase
Peroxidases
Sulfites
Superoxide dismutase
ISSN:1434-1948, 1099-0682
Online Access:Get full text
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Summary:A longstanding goal of biomimetic chemistry is the design and synthesis of functional enzyme mimics. The past three decades have seen a wide variety of materials, including metal complexes, polymers and other biomolecules, that mimic the structures and functions of naturally occurring enzymes. Among these, inorganic nanoparticles offer huge potential, because they are more stable than their natural counterparts, while having large surface areas and sizes comparable to those of natural enzymes. Therefore, a considerable number of “artificial enzymes” derived from inorganic nanomaterials have been reported. This microreview highlights the recent progress in the field of enzymatically active inorganic nanomaterials, including mimics of peroxidases, haloperoxidases, superoxide dismutases and sulfite oxidases, along with selected biotechnological applications and their future prospects. This microreview highlights the recent progress in the field of nanoparticles possessing enzyme‐like activities, including peroxidase, haloperoxidase, superoxide dismutase and sulfite oxidase mimics. Inorganic nanoparticles are more stable and cost‐efficient in synthesis than their natural counterparts, while exhibiting equally high enzymatic activities.
Bibliography:ark:/67375/WNG-SQHMZK10-5
istex:D1CFA2F58B368210924E4635A236D86723F55AF4
ArticleID:EJIC201501237
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1434-1948
1099-0682
DOI:10.1002/ejic.201501237