Reorganization Energy for Internal Electron Transfer in Multicopper Oxidases.
Hu, LiHong LU ; Farrokhnia, Maryam LU ; Heimdal, Jimmy LU ; Shleev, Sergey LU ; Rulisek, Lubomir LU and Ryde, Ulf LU
(2011)
In The Journal of Physical Chemistry Part B
115(Online September 28, 2011).
p.13111-13126
- Abstract
- We have calculated the reorganization energy for the intramolecular electron transfer between the reduced type 1 copper site and the peroxy intermediate of the trinuclear cluster in the multicopper oxidase CueO. The calculations are performed at the combined quantum mechanics and molecular mechanics (QM/MM) level, based on molecular dynamics simulations with tailored potentials for the two copper sites. We obtain a reorganization energy of 91-133 kJ/mol, depending on the theoretical treatment. The two Cu sites contribute by 12 and 22 kJ/mol to this energy, whereas the solvent contribution is 34 kJ/mol. The rest comes from the protein, involving small contributions from many residues. We have also estimated the energy difference between the... (More)
- We have calculated the reorganization energy for the intramolecular electron transfer between the reduced type 1 copper site and the peroxy intermediate of the trinuclear cluster in the multicopper oxidase CueO. The calculations are performed at the combined quantum mechanics and molecular mechanics (QM/MM) level, based on molecular dynamics simulations with tailored potentials for the two copper sites. We obtain a reorganization energy of 91-133 kJ/mol, depending on the theoretical treatment. The two Cu sites contribute by 12 and 22 kJ/mol to this energy, whereas the solvent contribution is 34 kJ/mol. The rest comes from the protein, involving small contributions from many residues. We have also estimated the energy difference between the two electron-transfer states and show that the reduction of the peroxy intermediate is exergonic by 43-87 kJ/mol, depending on the theoretical method. Both the solvent and the protein contribute to this energy difference, especially charged residues close to the two Cu sites. We compare these estimates with energies obtained from QM/MM optimizations and QM calculations in a vacuum and discuss differences between the results obtained at various levels of theory. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2201084
- author
- Hu, LiHong
LU
; Farrokhnia, Maryam
LU
; Heimdal, Jimmy
LU
; Shleev, Sergey
LU
; Rulisek, Lubomir
LU
and Ryde, Ulf
LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Part B
- volume
- 115
- issue
- Online September 28, 2011
- pages
- 13111 - 13126
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000296686000001
- pmid:21955325
- scopus:80855128956
- pmid:21955325
- ISSN
- 1520-5207
- DOI
- 10.1021/jp205897z
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039), Department of Chemistry (011001220)
- id
- 3603b768-7243-44f0-8097-5c9c53f7bafe (old id 2201084)
- date added to LUP
- 2016-04-01 13:02:23
- date last changed
- 2023-01-03 20:41:32
@article{3603b768-7243-44f0-8097-5c9c53f7bafe,
abstract = {{We have calculated the reorganization energy for the intramolecular electron transfer between the reduced type 1 copper site and the peroxy intermediate of the trinuclear cluster in the multicopper oxidase CueO. The calculations are performed at the combined quantum mechanics and molecular mechanics (QM/MM) level, based on molecular dynamics simulations with tailored potentials for the two copper sites. We obtain a reorganization energy of 91-133 kJ/mol, depending on the theoretical treatment. The two Cu sites contribute by 12 and 22 kJ/mol to this energy, whereas the solvent contribution is 34 kJ/mol. The rest comes from the protein, involving small contributions from many residues. We have also estimated the energy difference between the two electron-transfer states and show that the reduction of the peroxy intermediate is exergonic by 43-87 kJ/mol, depending on the theoretical method. Both the solvent and the protein contribute to this energy difference, especially charged residues close to the two Cu sites. We compare these estimates with energies obtained from QM/MM optimizations and QM calculations in a vacuum and discuss differences between the results obtained at various levels of theory.}},
author = {{Hu, LiHong and Farrokhnia, Maryam and Heimdal, Jimmy and Shleev, Sergey and Rulisek, Lubomir and Ryde, Ulf}},
issn = {{1520-5207}},
language = {{eng}},
number = {{Online September 28, 2011}},
pages = {{13111--13126}},
publisher = {{The American Chemical Society (ACS)}},
series = {{The Journal of Physical Chemistry Part B}},
title = {{Reorganization Energy for Internal Electron Transfer in Multicopper Oxidases.}},
url = {{https://lup.lub.lu.se/search/files/3123221/2338998.pdf}},
doi = {{10.1021/jp205897z}},
volume = {{115}},
year = {{2011}},
}