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Targeting the reactive intermediate in polysaccharide monooxygenases

Hedegård, Erik LU and Ryde, Ulf LU orcid (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)
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author
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organization
publishing date
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}},
}