Advanced

Targeting the reactive intermediate in polysaccharide monooxygenases

Hedegård, Erik LU and Ryde, Ulf LU (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:
author
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
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
2017-08-24 17:02:53
@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},
  keyword      = {Lytic polysaccharide monooxygenase,Density functional theory,Reaction mechanism ,Computational chemistry},
  language     = {eng},
  pages        = {9},
  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},
  year         = {2017},
}