Supramolecular Assembly of Artificial Metalloenzymes Based on the Dimeric Protein LmrR as Promiscuous Scaffold-Reference-Cited by-同舟云学术

Supramolecular Assembly of Artificial Metalloenzymes Based on the Dimeric Protein LmrR as Promiscuous Scaffold

Published:2015-08-04 Issue:31 Volume:137 Page:9796-9799
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bos Jeffrey¹,Browne Wesley R.¹,Driessen Arnold J. M.²,Roelfes Gerard¹

Affiliation:

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

2. Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 7, 9747 AG, Groningen, The Netherlands

Funder

Dutch National Research School Combination Catalysis Controlled by Chemical Design

European Research Council

Biotechnology based Ecologically Balanced Sustainable Industrial Consortium

Ministerie van Onderwijs, Cultuur en Wetenschap

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b05790

Reference32 articles.

1. Artificial metalloenzymes for enantioselective catalysis

2. Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis

3. Artificial Metalloenzymes

4. Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium(I) moiety

5. Toward the Computational Design of Artificial Metalloenzymes: From Protein–Ligand Docking to Multiscale Approaches

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