Light‐induced uncaging for time‐resolved observations of biochemical reactions by MAS NMR spectroscopy

  • Light‐induced activation of biomolecules by uncaging of photolabile protection groups has found many applications for triggering biochemical reactions with minimal perturbations directly within cells. Such an approach might also offer unique advantages for solid‐state NMR experiments on membrane proteins for initiating reactions within or at the membrane directly within the closed MAS rotor. Herein, we demonstrate that the integral membrane protein E. coli diacylglycerol kinase (DgkA), which catalyzes the phosphorylation of diacylglycerol, can be controlled by light under MAS‐NMR conditions. Uncaging of NPE‐ATP or of lipid substrate NPE‐DOG by in situ illumination triggers its enzymatic activity, which can be monitored by real‐time 31P‐MAS NMR. This proof‐of‐concept illustrates that combining MAS‐NMR with uncaging strategies and illumination methods offers new possibilities for controlling biochemical reactions at or within lipid bilayers.

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Author:Julian Martinus de Mos, Andreas Jakob, Johanna Becker-Baldus, Alexander HeckelORCiD, Clemens Glaubitz
Pubmed Id:
Parent Title (German):Chemistry - a European journal
Place of publication:Weinheim
Document Type:Article
Date of Publication (online):2020/05/13
Date of first Publication:2020/04/02
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2020/11/11
Tag:DgkA; NMR spectroscopy; caged ATP; caged diacylglycerol; enzymes; solid-state NMR
Page Number:4
First Page:6789
Last Page:6792
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0