Is density functional theory accurate for lytic polysaccharide monooxygenase enzymes
(2020) In Dalton Transactions 49(5). p.1501-1512- Abstract
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... (More)
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).
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- author
- Larsson, Ernst D. LU ; Dong, Geng LU ; Veryazov, Valera LU ; Ryde, Ulf LU and Hedegård, Erik D. LU
- organization
- publishing date
- 2020-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Dalton Transactions
- volume
- 49
- issue
- 5
- pages
- 12 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- pmid:31922155
- scopus:85079075133
- ISSN
- 1477-9226
- DOI
- 10.1039/c9dt04486h
- language
- English
- LU publication?
- yes
- id
- 9933159b-b197-41a6-9dbf-8aac97fd987a
- date added to LUP
- 2020-03-02 11:27:33
- date last changed
- 2024-04-17 04:35:12
@article{9933159b-b197-41a6-9dbf-8aac97fd987a, abstract = {{<p>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. [CuO<sub>2</sub>]<sup>+</sup>, [CuO]<sup>+</sup> and [CuOH]<sup>2+</sup>) 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).</p>}}, author = {{Larsson, Ernst D. and Dong, Geng and Veryazov, Valera and Ryde, Ulf and Hedegård, Erik D.}}, issn = {{1477-9226}}, language = {{eng}}, month = {{01}}, number = {{5}}, pages = {{1501--1512}}, publisher = {{Royal Society of Chemistry}}, series = {{Dalton Transactions}}, title = {{Is density functional theory accurate for lytic polysaccharide monooxygenase enzymes}}, url = {{http://dx.doi.org/10.1039/c9dt04486h}}, doi = {{10.1039/c9dt04486h}}, volume = {{49}}, year = {{2020}}, }