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Directed Evolution of Iridium-Substituted Myoglobin Affords Versatile Artificial Metalloenzymes for Enantioselective C−C Bond-Forming Reactions

Ward, Thomas R.. (2016) Directed Evolution of Iridium-Substituted Myoglobin Affords Versatile Artificial Metalloenzymes for Enantioselective C−C Bond-Forming Reactions. Angewandte Chemie International Edition, 55 (48). pp. 14909-14911.

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Official URL: http://edoc.unibas.ch/53740/

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Abstract

Upgrading myoglobin with iridium : A metal-substitution strategy has been used to afford a repurposed myoglobin for challenging cyclopropanation and intramolecular C−H activation reactions. The performance of the iridium-loaded myoglobin (orange sphere) was improved through directed evolution of eight active-site residues (yellow surface).
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:1433-7851
e-ISSN:1521-3773
Note:Publication type according to Uni Basel Research Database: Journal article -- The final publication is available at Wiley, see DOI link
Language:English
Identification Number:
Last Modified:17 Aug 2018 12:52
Deposited On:01 Feb 2017 11:09

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