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Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme

Okamoto, Yasunori and Köhler, Valentin and Paul, Caroline E. and Hollmann, Frank and Ward, Thomas R.. (2016) Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme. ACS Catalysis, 6 (6). pp. 3553-3557.

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Official URL: http://edoc.unibas.ch/53490/

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Abstract

NADH mimics (mNADHs) have been shown to accelerate and orthogonally activate ene reductase-catalyzed reactions. However, existing regeneration methods of NAD(P)H fail for mNADHs. Catalysis with artificial metalloenzymes based on streptavidin (Sav) variants and a biotinylated iridium cofactor enable mNADH regeneration with formate. This regeneration can be coupled with ene reductase-catalyzed asymmetric reduction of α,β-unsaturated compounds, because of the protective compartmentalization of the organometallic cofactor. With 10 mol % mNAD+, a preparative scale reaction (>100 mg) gave full conversion with 98% ee, where TTNs reached 2000, with respect to the Ir cofactor under ambient atmosphere in aqueous medium.
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Okamoto, Yasunori and Köhler, Valentin and Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
e-ISSN:2155-5435
Note:Publication type according to Uni Basel Research Database: Journal article -- The final publication is available at ACS, see DOI link
Language:English
Identification Number:
Last Modified:17 Aug 2018 12:49
Deposited On:01 Feb 2017 11:07

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