Correlating Experiment and Theory for Electron Paramagnetic Resonance and Substrate Binding in a Lytic Polysaccharide Monooxygenase

22 October 2020, Version 2
This content is a preprint and has not undergone peer review at the time of posting.


Lytic polysaccharide monooxygenases (LPMOs) are enzymes that binds polysaccharides followed by an (oxidative) disruption of the polysaccharide surface, thereby boosting depolymerization. The binding process between LPMO and polysaccharide is key to the mechanism and recent investigations have established structure-function relationships for this binding, employing hyperfine coupling constants (HFCs) from EPR spectroscopy. Unfortunately, EPR does not provide direct structural data and therefore the experimental EPR parameters have been supported with parameters cal-
culated with density functional theory. Yet, calculated HFCs are extremely sensitive
to the employed computational setup. Using the LPMO Ls(AA9)A, we here quantify
the importance of several choices in the computational setup, ranging from the use
of specialized basis, the underlying structures, and the employed exchange–correlation
functional. We compare our results to both X-ray structures and experiment (EPR spectra) for Ls(AA9)A as well as to recent experimental/theoretical results for another
(AA10) family of LPMOs.



Supplementary materials

main SI


Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.