edoc

An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades

Okamoto, Yasunori and Köhler, Valentin and Ward, Thomas R.. (2016) An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades. Journal of the American Chemical Society, 138 (18). pp. 5782-5784.

[img] PDF - Accepted Version
938Kb

Official URL: http://edoc.unibas.ch/53912/

Downloads: Statistics Overview

Abstract

Enzymes typically depend on either NAD(P)H or FADH 2 as hydride source for reduction purposes. In contrast, organometallic catalysts most often rely on isopropanol or formate to generate the reactive hydride moiety. Here we show that incorporation of a Cp*Ir cofactor possessing a biotin moiety and 4,7-dihydroxy-1,10-phenanthroline into streptavidin yields an NAD(P)H-dependent artificial transfer hydrogenase (ATHase). This ATHase (0.1 mol%) catalyzes imine reduction with 1 mM NADPH (2 mol%), which can be concurrently regenerated by a glucose dehydrogenase (GDH) using only 1.2 equiv of glucose. A four-enzyme cascade consisting of the ATHase, the GDH, a monoamine oxidase, and a catalase leads to the production of enantiopure amines.
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
ISSN:0002-7863
e-ISSN:1520-5126
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 12:58
Deposited On:01 Feb 2017 12:31

Repository Staff Only: item control page