Issue 45, 2008
From the journal:

Physical Chemistry Chemical Physics

A view on phosphate ester photochemistry by time-resolved solid state NMR. Intramolecular redox reaction of caged ATP

Alexey V. Cherepanov,*ab   Elena V. Doroshenko,ab   Jörg Matysik,a   Simon de Vriesb  and  Huub J. M. De Groota  

* Corresponding authors

a Biophysical Organic Chemistry/Solid State NMR group, Leiden Institute of Chemistry, Faculty of Mathematics and Natural Sciences, Leiden University, Einsteinweg 55, Leiden, The Netherlands
E-mail: a.cherepanov@chem.leidenuniv.nl
Fax: +31715274603
Tel: +31715274539

b Section of Enzymology, Department of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, Julianalaan 67, Delft, The Netherlands
E-mail: a.v.cherepanov@tudelft.nl
Fax: +31152782355
Tel: +31152781625

Abstract

The light-driven intramolecular redox reaction of adenosine-5′-triphosphate-[P3-(1-(2-nitrophenyl)-ethyl)]ester (caged ATP) has been studied in frozen aqueous solution using time-resolved solid state NMR spectroscopy under continuous illumination conditions. Cleavage of the phosphate ester bond leads to 0.3, 1.36, and 6.06 ppm downfield shifts of the α-, β-, and γ-phosphorus resonances of caged ATP, respectively. The observed rate of ATP formation is 2.4 ± 0.2 h−1 at 245 K. The proton released in the reaction binds to the triphosphate moiety of the nascent ATP, causing the upfield shifts of the 31P resonances. Analyses of the reaction kinetics indicate that bond cleavage and proton release are two sequential processes in the solid state, suggesting that the 1-hydroxy,1-(2-nitrosophenyl)-ethyl carbocation intermediate is involved in the reaction. The β-phosphate oxygen atom of ATP is protonated first, indicating its proximity to the reaction center, possibly within hydrogen bonding distance. The residual linewidth kinetics are interpreted in terms of chemical exchange processes, hydrogen bonding of the β-phosphate oxygen atom and evolution of the hydrolytic equilibrium at the triphosphate moiety of the nascent ATP. Photoreaction of caged ATPin situ gives an opportunity to study structural kinetics and catalysis of ATP-dependent enzymes by NMR spectroscopy in rotating solids.

Graphical abstract: A view on phosphate ester photochemistry by time-resolved solid state NMR. Intramolecular redox reaction of caged ATP

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Article information

DOI
https://doi.org/10.1039/B806677A
Article type
Paper
Submitted
21 Apr 2008
Accepted
11 Aug 2008
First published
08 Oct 2008

Phys. Chem. Chem. Phys., 2008,10, 6820-6828

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A view on phosphate ester photochemistry by time-resolved solid state NMR. Intramolecular redox reaction of caged ATP

A. V. Cherepanov, E. V. Doroshenko, J. Matysik, S. D. Vries and H. J. M. De Groot, Phys. Chem. Chem. Phys., 2008, 10, 6820 DOI: 10.1039/B806677A

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