An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades
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- 作者：Yasunori Okamoto ; Valentin Köhler ; Thomas R. Ward
- 刊名：Journal of the American Chemical Society
- 出版年：2016
- 出版时间：May 11, 2016
- 年：2016
- 卷：138
- 期：18
- 页码：5781-5784
- 全文大小：251K
- 年卷期：0
- ISSN：1520-5126
文摘
Enzymes typically depend on either NAD(P)H or FADH2 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.