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High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR. / Varghese, Sabu; Halling, Peter J.; Häussinger, Daniel et al.
In: The Journal of Physical Chemistry C, Vol. 120, No. 50, 22.12.2016, p. 28717-28726.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Varghese, S, Halling, PJ, Häussinger, D & Wimperis, S 2016, 'High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR', The Journal of Physical Chemistry C, vol. 120, no. 50, pp. 28717-28726. https://doi.org/10.1021/acs.jpcc.6b11575

APA

Varghese, S., Halling, P. J., Häussinger, D., & Wimperis, S. (2016). High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR. The Journal of Physical Chemistry C, 120(50), 28717-28726. https://doi.org/10.1021/acs.jpcc.6b11575

Vancouver

Varghese S, Halling PJ, Häussinger D, Wimperis S. High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR. The Journal of Physical Chemistry C. 2016 Dec 22;120(50):28717-28726. Epub 2016 Nov 25. doi: 10.1021/acs.jpcc.6b11575

Author

Varghese, Sabu ; Halling, Peter J. ; Häussinger, Daniel et al. / High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR. In: The Journal of Physical Chemistry C. 2016 ; Vol. 120, No. 50. pp. 28717-28726.

Bibtex

@article{57a4fee55f0e41e09d262e2b6e35542a,
title = "High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR",
abstract = "Solid-state magic-angle spinning (MAS) NMR spectroscopy was employed to investigate structural detail in an enzyme, hu- man carbonic anhydrase II (hCA II) in uniformly 15N and selectively (15N 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. Based on the one- and two-dimensional 1H, 13C, 15N and 29Si MAS NMR spectra, chemical shift assignments could be obtained from the silica support, covalent linker and the 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 sup- port. 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.",
author = "Sabu Varghese and Halling, {Peter J.} and Daniel H{\"a}ussinger and Stephen Wimperis",
year = "2016",
month = dec,
day = "22",
doi = "10.1021/acs.jpcc.6b11575",
language = "English",
volume = "120",
pages = "28717--28726",
journal = "The Journal of Physical Chemistry C",
issn = "1932-7447",
publisher = "American Chemical Society",
number = "50",

}

RIS

TY - JOUR

T1 - High-resolution structural characterization of a heterogeneous biocatalyst using solid-state NMR

AU - Varghese, Sabu

AU - Halling, Peter J.

AU - Häussinger, Daniel

AU - Wimperis, Stephen

PY - 2016/12/22

Y1 - 2016/12/22

N2 - Solid-state magic-angle spinning (MAS) NMR spectroscopy was employed to investigate structural detail in an enzyme, hu- man carbonic anhydrase II (hCA II) in uniformly 15N and selectively (15N 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. Based on the one- and two-dimensional 1H, 13C, 15N and 29Si MAS NMR spectra, chemical shift assignments could be obtained from the silica support, covalent linker and the 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 sup- port. 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.

AB - Solid-state magic-angle spinning (MAS) NMR spectroscopy was employed to investigate structural detail in an enzyme, hu- man carbonic anhydrase II (hCA II) in uniformly 15N and selectively (15N 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. Based on the one- and two-dimensional 1H, 13C, 15N and 29Si MAS NMR spectra, chemical shift assignments could be obtained from the silica support, covalent linker and the 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 sup- port. 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.

U2 - 10.1021/acs.jpcc.6b11575

DO - 10.1021/acs.jpcc.6b11575

M3 - Journal article

VL - 120

SP - 28717

EP - 28726

JO - The Journal of Physical Chemistry C

JF - The Journal of Physical Chemistry C

SN - 1932-7447

IS - 50

ER -