Towards resolving the complex paramagnetic nuclear magnetic resonance (NMR) spectrum of small laccase: assignments of resonances to residue-specific nuclei

Dasgupta, Rubin; Gupta, Karthick B. S. S.; de Groot, Huub J. M.; Ubbink, Marcellus

doi:https://doi.org/10.5194/mr-2-15-2021

Articles | Volume 2, issue 1

https://doi.org/10.5194/mr-2-15-2021

© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.

Special issue:

Robert Kaptein Festschrift

https://doi.org/10.5194/mr-2-15-2021

© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.

Articles | Volume 2, issue 1

Research article

|

29 Jan 2021

Research article |

| 29 Jan 2021

Towards resolving the complex paramagnetic nuclear magnetic resonance (NMR) spectrum of small laccase: assignments of resonances to residue-specific nuclei

Rubin Dasgupta, Karthick B. S. S. Gupta, Huub J. M. de Groot, and Marcellus Ubbink

Supplement

https://doi.org/10.5194/mr-2-15-2021-supplement

Data sets

Towards resolving the complex paramagnetic NMR spectrum of small laccase: Assignments of resonances to residue specific nuclei Rubin Dasgupta, Karthick B. S. S. Gupta, Huub J. M. de Groot, and Marcellus Ubbink https://doi.org/10.5281/zenodo.4392869

Short summary

A method is demonstrated that can help in sequence-specific NMR signal assignment to nuclear spins near a strongly paramagnetic metal in an enzyme. A combination of paramagnetically tailored NMR experiments and second-shell mutagenesis was used to attribute previously observed chemical exchange processes in the active site of laccase to specific histidine ligands. The signals of nuclei close to the metal can be used as spies to unravel the role of motions in the catalytic process.