Is density functional theory accurate for lytic polysaccharide monooxygenase enzymes?

Ernst D. Larsson, Geng Dong, Valera Veryazov, Ulf Ryde, Erik D. Hedegård*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review


The lytic polysaccharide monooxygenase (LPMO) enzymes boost polysaccharide depolymerization through oxidative chemistry, which has fueled the hope for more energy-efficient production of biofuel. We have recently proposed a mechanism for the oxidation of the polysaccharide substrate (E. D. Hedegård and U. Ryde, Chem. Sci., 2018, 9, 3866–3880). In this mechanism, intermediates with superoxide, oxyl, as well as hydroxyl (i.e. [CuO2]+, [CuO]+ and [CuOH]2+) cores were involved. These complexes can have both singlet and triplet spin states, and both spin-states may be important for how LPMOs function during catalytic turnover. Previous calculations on LPMOs have exclusively been based on density functional theory (DFT). However, different DFT functionals are known to display large differences for spin-state splittings in transition-metal complexes, and this has also been an issue for LPMOs. In this paper, we study the accuracy of DFT for spin-state splittings in superoxide, oxyl, and hydroxyl intermediates involved in LPMO turnover. As reference we employ multiconfigurational perturbation theory (CASPT2).
Original languageEnglish
JournalDalton Transactions
Issue number5
Pages (from-to)1501-1512
Publication statusPublished - 7. Feb 2020
Externally publishedYes


Dive into the research topics of 'Is density functional theory accurate for lytic polysaccharide monooxygenase enzymes?'. Together they form a unique fingerprint.

Cite this