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Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H

Quinto, Tommaso and Köhler, Valentin and Häussinger, Daniel and Ward, Thomas R.. (2015) Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H. Organic and Biomolecular Chemistry, 13. pp. 357-360.

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Official URL: http://edoc.unibas.ch/40389/

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Abstract

Stereoselectively labelled isotopomers of NAD(P)H are highly relevant for mechanistic studies of enzymes which utilize them as redox equivalents. Whereas several methods are firmly established for their generation in high diastereomeric purity by enzymatic methods, alternative methods have so far not been investigated. The article presents the stereoselective deuteration of NAD+ at the 4-position (90% de) of the pyridinium-ring by means of an artificial metalloenzyme. The artificial metalloenzyme consists of a biotinylated iridium cofactor embedded in streptavidin isoforms and the resulting constructs have been previously shown to be compatible with natural enzymes. Alternative methods for stereoselective NAD(P)+ reduction are expected to be of high interest for the mechanistic study of enzymes that accept NAD(P)H mimics and for the synthesis of structurally related fine chemicals.
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
05 Faculty of Science > Departement Chemie > Chemie > Nuclear Magnetic Resonance (Häussinger)
UniBasel Contributors:Quinto, Tommaso and Köhler, Valentin and Ward, Thomas R. and Häussinger, Daniel
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Royal Society of Chemistry
ISSN:1477-0520
e-ISSN:1477-0539
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:03 May 2017 08:28
Deposited On:03 May 2016 13:54

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