Targeting the reactive intermediate in polysaccharide monooxygenases
(2017) In Journal of Biological Inorganic Chemistry- Abstract
- Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making them interesting for the production of biofuel from cellulose. However, the details of this activation are unknown; in particular, the nature of the intermediate that attacks the glycoside C–H bond in the polysaccharide is not known, and a number of different species have been suggested. The homolytic bond-dissociation energy (BDE) has often been used as a descriptor for the bond-activation power, especially for inorganic model complexes. We have employed quantum-chemical cluster calculations to estimate the BDE for a number of possible LPMO intermediates to bridge the gap between... (More)
- Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making them interesting for the production of biofuel from cellulose. However, the details of this activation are unknown; in particular, the nature of the intermediate that attacks the glycoside C–H bond in the polysaccharide is not known, and a number of different species have been suggested. The homolytic bond-dissociation energy (BDE) has often been used as a descriptor for the bond-activation power, especially for inorganic model complexes. We have employed quantum-chemical cluster calculations to estimate the BDE for a number of possible LPMO intermediates to bridge the gap between model complexes and the actual LPMO active site. The calculated BDEs suggest that the reactive intermediate is either a Cu(II)–oxyl, a Cu(III)–oxyl, or a Cu(III)–hydroxide, which indicate that O–O bond breaking occurs before the C–H activation step. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/37a5d70f-389f-41cf-8664-2c57fd6b40c3
- author
- Hedegård, Erik
LU
and Ryde, Ulf
LU
- organization
- publishing date
- 2017
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Lytic polysaccharide monooxygenase, Density functional theory, Reaction mechanism, Computational chemistry
- in
- Journal of Biological Inorganic Chemistry
- pages
- 9 pages
- publisher
- Springer
- external identifiers
-
- scopus:85023202713
- pmid:28698982
- wos:000411902700004
- ISSN
- 0949-8257
- DOI
- 10.1007/s00775-017-1480-1
- language
- English
- LU publication?
- yes
- id
- 37a5d70f-389f-41cf-8664-2c57fd6b40c3
- alternative location
- https://link.springer.com/article/10.1007%2Fs00775-017-1480-1
- date added to LUP
- 2017-07-27 14:43:25
- date last changed
- 2023-04-07 20:13:07
@article{37a5d70f-389f-41cf-8664-2c57fd6b40c3, abstract = {{Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making them interesting for the production of biofuel from cellulose. However, the details of this activation are unknown; in particular, the nature of the intermediate that attacks the glycoside C–H bond in the polysaccharide is not known, and a number of different species have been suggested. The homolytic bond-dissociation energy (BDE) has often been used as a descriptor for the bond-activation power, especially for inorganic model complexes. We have employed quantum-chemical cluster calculations to estimate the BDE for a number of possible LPMO intermediates to bridge the gap between model complexes and the actual LPMO active site. The calculated BDEs suggest that the reactive intermediate is either a Cu(II)–oxyl, a Cu(III)–oxyl, or a Cu(III)–hydroxide, which indicate that O–O bond breaking occurs before the C–H activation step.}}, author = {{Hedegård, Erik and Ryde, Ulf}}, issn = {{0949-8257}}, keywords = {{Lytic polysaccharide monooxygenase; Density functional theory; Reaction mechanism; Computational chemistry}}, language = {{eng}}, publisher = {{Springer}}, series = {{Journal of Biological Inorganic Chemistry}}, title = {{Targeting the reactive intermediate in polysaccharide monooxygenases}}, url = {{http://dx.doi.org/10.1007/s00775-017-1480-1}}, doi = {{10.1007/s00775-017-1480-1}}, year = {{2017}}, }