On the role of strain in blue copper proteins
Ryde, Ulf LU
; Olsson, Mats H M
LU
; Roos, Björn O.
LU
; De Kerpel, Jan O A
and Pierloot, Kristine
(2000)
In Journal of Biological Inorganic Chemistry
5(5).
p.565-574
- Abstract
Theoretical investigations of the structure and function of the blue copper proteins are described. We have studied the optimum vacuum geometry of oxidised and reduced copper sites, the relative stability of trigonal and tetragonal Cu(II) structures, the relation between the structure and electronic spectra, the reorganisation energy, and reduction potentials. Our calculations give no support to the suggestion that strain plays a significant role in the function of these proteins; on the contrary, our results show that the structures encountered in the proteins are close to their optimal vacuum geometries (within 7 kJ/mol). We stress the importance of defining what is meant by strain and of quantifying strain energies or forces in order... (More)
Theoretical investigations of the structure and function of the blue copper proteins are described. We have studied the optimum vacuum geometry of oxidised and reduced copper sites, the relative stability of trigonal and tetragonal Cu(II) structures, the relation between the structure and electronic spectra, the reorganisation energy, and reduction potentials. Our calculations give no support to the suggestion that strain plays a significant role in the function of these proteins; on the contrary, our results show that the structures encountered in the proteins are close to their optimal vacuum geometries (within 7 kJ/mol). We stress the importance of defining what is meant by strain and of quantifying strain energies or forces in order to make strain hypotheses testable.
(Less)
- author
- Ryde, Ulf
LU
; Olsson, Mats H M
LU
; Roos, Björn O.
LU
; De Kerpel, Jan O A
and Pierloot, Kristine
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Blue copper proteins, Entatic state theory, Induced-rack theory, Protein strain, Quantum chemical calculations
- in
- Journal of Biological Inorganic Chemistry
- volume
- 5
- issue
- 5
- pages
- 10 pages
- publisher
- Springer
- external identifiers
-
- pmid:11085647
- scopus:0033788007
- ISSN
- 0949-8257
- DOI
- 10.1007/s007750000147
- language
- English
- LU publication?
- yes
- id
- 19b96888-bdeb-42bb-aeb0-2bbd9de82c5b
- date added to LUP
- 2017-02-04 11:43:04
- date last changed
- 2024-01-13 13:01:13
@article{19b96888-bdeb-42bb-aeb0-2bbd9de82c5b,
abstract = {{<p>Theoretical investigations of the structure and function of the blue copper proteins are described. We have studied the optimum vacuum geometry of oxidised and reduced copper sites, the relative stability of trigonal and tetragonal Cu(II) structures, the relation between the structure and electronic spectra, the reorganisation energy, and reduction potentials. Our calculations give no support to the suggestion that strain plays a significant role in the function of these proteins; on the contrary, our results show that the structures encountered in the proteins are close to their optimal vacuum geometries (within 7 kJ/mol). We stress the importance of defining what is meant by strain and of quantifying strain energies or forces in order to make strain hypotheses testable.</p>}},
author = {{Ryde, Ulf and Olsson, Mats H M and Roos, Björn O. and De Kerpel, Jan O A and Pierloot, Kristine}},
issn = {{0949-8257}},
keywords = {{Blue copper proteins; Entatic state theory; Induced-rack theory; Protein strain; Quantum chemical calculations}},
language = {{eng}},
number = {{5}},
pages = {{565--574}},
publisher = {{Springer}},
series = {{Journal of Biological Inorganic Chemistry}},
title = {{On the role of strain in blue copper proteins}},
url = {{https://lup.lub.lu.se/search/files/135489968/38_commentary.pdf}},
doi = {{10.1007/s007750000147}},
volume = {{5}},
year = {{2000}},
}