The cupric geometry of blue copper proteins is not strained
Ryde, Ulf LU
; Olsson, Mats H M
LU
; Pierloot, Kristine
and Roos, Björn O.
LU
(1996)
In Journal of Molecular Biology
261(4).
p.586-596
- Abstract
The geometry of several realistic models of the metal coordination sphere in the blue copper proteins has been optimised using high-level quantum chemical methods. The results show that the optimal vacuum structure of the Cu(II) models is virtually identical to the crystal structure of oxidised blue copper proteins. For the reduced forms, the optimised structure seems to be more tetrahedral than the one found in the proteins, but the energy difference between the two geometries is less than 5 kJ/mol, i.e. within the error limits of the method. Thus, the results raise strong doubts against hypotheses (entatic state and the induced-rack theory) suggesting that blue copper proteins force the oxidised metal coordination sphere into a... (More)
The geometry of several realistic models of the metal coordination sphere in the blue copper proteins has been optimised using high-level quantum chemical methods. The results show that the optimal vacuum structure of the Cu(II) models is virtually identical to the crystal structure of oxidised blue copper proteins. For the reduced forms, the optimised structure seems to be more tetrahedral than the one found in the proteins, but the energy difference between the two geometries is less than 5 kJ/mol, i.e. within the error limits of the method. Thus, the results raise strong doubts against hypotheses (entatic state and the induced-rack theory) suggesting that blue copper proteins force the oxidised metal coordination sphere into a structure similar to that preferred by Cu(I) in order to minimise the reorganisation energy of the electron transfer reaction. Instead, a small reorganisation energy seems to be reached by an appropriate choice of metal ligands. In particular, the cysteine thiolate ligand appears to be crucial, changing the preferred geometry of the oxidised complexes from square-planar to a more trigonal geometry.
(Less)
- author
- Ryde, Ulf
LU
; Olsson, Mats H M
LU
; Pierloot, Kristine
and Roos, Björn O.
LU
- organization
- publishing date
- 1996-08-30
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- B3LYP method, Blue copper protein, Entatic state theory, Induced-rack theory, Protein strain
- in
- Journal of Molecular Biology
- volume
- 261
- issue
- 4
- pages
- 11 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0030606884
- pmid:8794878
- ISSN
- 0022-2836
- DOI
- 10.1006/jmbi.1996.0484
- language
- English
- LU publication?
- yes
- id
- e6b1cce4-bc0a-4992-9494-624a8e72cba5
- date added to LUP
- 2017-02-04 11:31:47
- date last changed
- 2025-01-07 06:05:07
@article{e6b1cce4-bc0a-4992-9494-624a8e72cba5,
abstract = {{<p>The geometry of several realistic models of the metal coordination sphere in the blue copper proteins has been optimised using high-level quantum chemical methods. The results show that the optimal vacuum structure of the Cu(II) models is virtually identical to the crystal structure of oxidised blue copper proteins. For the reduced forms, the optimised structure seems to be more tetrahedral than the one found in the proteins, but the energy difference between the two geometries is less than 5 kJ/mol, i.e. within the error limits of the method. Thus, the results raise strong doubts against hypotheses (entatic state and the induced-rack theory) suggesting that blue copper proteins force the oxidised metal coordination sphere into a structure similar to that preferred by Cu(I) in order to minimise the reorganisation energy of the electron transfer reaction. Instead, a small reorganisation energy seems to be reached by an appropriate choice of metal ligands. In particular, the cysteine thiolate ligand appears to be crucial, changing the preferred geometry of the oxidised complexes from square-planar to a more trigonal geometry.</p>}},
author = {{Ryde, Ulf and Olsson, Mats H M and Pierloot, Kristine and Roos, Björn O.}},
issn = {{0022-2836}},
keywords = {{B3LYP method; Blue copper protein; Entatic state theory; Induced-rack theory; Protein strain}},
language = {{eng}},
month = {{08}},
number = {{4}},
pages = {{586--596}},
publisher = {{Elsevier}},
series = {{Journal of Molecular Biology}},
title = {{The cupric geometry of blue copper proteins is not strained}},
url = {{https://lup.lub.lu.se/search/files/135489357/21_pcstr.pdf}},
doi = {{10.1006/jmbi.1996.0484}},
volume = {{261}},
year = {{1996}},
}