LmrR: A Privileged Scaffold for Artificial Metalloenzymes-Reference-Cited by-同舟云学术

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LmrR: A Privileged Scaffold for Artificial Metalloenzymes

Published:2019-02-22 Issue:3 Volume:52 Page:545-556
ISSN:0001-4842
Container-title:Accounts of Chemical Research
language:en
Short-container-title:Acc. Chem. Res.

Author:

Roelfes Gerard¹^ORCID

Affiliation:

1. Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Funder

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Ministerie van Onderwijs, Cultuur en Wetenschap

FP7 Ideas: European Research Council

Netherlands Research School Combination Catalysis

Publisher

American Chemical Society (ACS)

Subject

General Medicine,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.accounts.9b00004

Reference43 articles.

1. Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

2. Chemomimetic Biocatalysis: Exploiting the Synthetic Potential of Cofactor-Dependent Enzymes To Create New Catalysts

3. Computational Enzyme Design

4. The coming of age of de novo protein design

5. Expanding the Enzyme Universe: Accessing Non-Natural Reactions by Mechanism-Guided Directed Evolution

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5. Design and Evolution of an Artificial Friedel–Crafts Alkylation Enzyme Featuring an Organoboronic Acid Residue;Journal of the American Chemical Society;2024-08-27

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