High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR

Varghese, Sabu and Halling, Peter J. and Häussinger, Daniel and Wimperis, Stephen. (2016) High-Resolution Structural Characterization of a Heterogeneous Biocatalyst Using Solid-State NMR. Journal of Physical Chemistry C, 120 (50). pp. 28717-28726.

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Official URL: http://edoc.unibas.ch/58692/

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Solid-state magic-angle spinning (MAS) NMR spectroscopy was employed to investigate structural detail in the enzyme human carbonic anhydrase II (hCA II) in uniformly N-15 and selectively (N-15 leucine) enriched states, covalently immobilized on epoxy-functionalized silica. The immobilized hCA II retained 71% of its specific enzymatic activity when compared to the free enzyme in solution. On the basis of the one- and two-dimensional H-1, C-13, N-15, and Si-29 MAS NMR. spectra, chemical shift assignments could be obtained from the silica support, covalent linker, and immobilized enzyme. The successful covalent immobilization of the enzyme on epoxy silica was confirmed by the appearance of signals from the aromatic and carbonyl groups in the immobilized enzyme in addition to signals from the modified support. Most notably, our MAS NMR results suggest that the covalent immobilization of the hCA II on epoxy silica does not significantly affect the structural integrity of the protein.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Nuclear Magnetic Resonance (Häussinger)
UniBasel Contributors:Häussinger, Daniel
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:30 Jun 2020 13:12
Deposited On:15 Jan 2018 08:49

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