Data Entry: Please note that the research database will be replaced by UNIverse by the end of October 2023. Please enter your data into the system https://universe-intern.unibas.ch. Thanks

Login for users with Unibas email account...

Login for registered users without Unibas email account...

 
Artificial Metalloenzymes: Reaction Scope and Optimization Strategies
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4196692
Author(s) Schwizer, Fabian; Okamoto, Yasunori; Heinisch, Tillmann; Gu, Yifan; Pellizzoni, Michela M.; Lebrun, Vincent; Reuter, Raphael; Köhler, Valentin; Lewis, Jared C.; Ward, Thomas R.
Author(s) at UniBasel Ward, Thomas R.
Schwizer, Fabian
Okamoto, Yasunori
Heinisch, Tillmann
Pellizzoni, Michela Maria
Lebrun, Vincent
Reuter, Raphael
Köhler, Valentin
Year 2018
Year: comment 2018
Title Artificial Metalloenzymes: Reaction Scope and Optimization Strategies
Journal Chemical Reviews
Volume 118
Number 1
Pages / Article-Number 142-231
Mesh terms Alkylation; Animals; Biocatalysis; Humans; Hydrogenation; Imines, metabolism; Ketones, metabolism; Metalloproteins, metabolism; Oxidoreductases, metabolism; Protein Engineering
Abstract The incorporation of a synthetic, catalytically competent metallocofactor into a protein scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late 1970’s. Progress in the ensuing years was limited by the tools available for both organometallic synthesis and protein engineering. Advances in both of these areas, combined with increased appreciation of the potential benefits of combining attractive features of both homogeneous catalysis and enzymatic catalysis, led to a resurgence of interest in ArMs starting in the early 2000’s. Perhaps the most intriguing of potential ArM properties is their ability to endow homogeneous catalysts with a genetic memory. Indeed, incorporating a homogeneous catalyst into a genetically encoded scaffold offers the opportunity to improve ArM performance by directed evolution. This capability could, in turn, lead to improvements in ArM efficiency similar to those obtained for natural enzymes, providing systems suitable for practical applications and greater insight into the role of second coordination sphere interactions in organometallic catalysis. Since its renaissance in the early 2000’s, different aspects of artificial metalloenzymes have been extensively reviewed and highlighted. Our intent is to provide a comprehensive overview of all work in the field up to December 2016, organized according to reaction class. Because of the wide range of non-natural reactions catalyzed by ArMs, this was done using a functional-group transformation classification. The review begins with a summary of the proteins and the anchoring strategies used to date for the creation of ArMs, followed by a historical perspective. Then follows a summary of the reactions catalyzed by ArMs and a concluding critical outlook. This analysis allows for comparison of similar reactions catalyzed by ArMs constructed using different metallocofactor anchoring strategies, cofactors, protein scaffolds, and mutagenesis strategies. These data will be used to construct a searchable Web site on ArMs that will be updated regularly by the authors.
Publisher American Chemical Society
ISSN/ISBN 0009-2665 ; 1520-6890
edoc-URL http://edoc.unibas.ch/59074/
Full Text on edoc Available
Digital Object Identifier DOI 10.1021/acs.chemrev.7b00014
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/28714313
ISI-Number WOS:000419999700005
Document type (ISI) Journal Article, Review
 
   

MCSS v5.8 PRO. 0.347 sec, queries - 0.000 sec ©Universität Basel  |  Impressum   |    
28/03/2024