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Issue 2, 2015
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Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H

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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.

Graphical abstract: Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H

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Publication details

The article was received on 29 Sep 2014, accepted on 30 Oct 2014 and first published on 07 Nov 2014


Article type: Communication
DOI: 10.1039/C4OB02071E
Citation: Org. Biomol. Chem., 2015,13, 357-360
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    Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H

    T. Quinto, D. Häussinger, V. Köhler and T. R. Ward, Org. Biomol. Chem., 2015, 13, 357
    DOI: 10.1039/C4OB02071E

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