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Density functional study on UV/VIS spectra of copper-protein active sites: the effect of mutations

UV/VIS Electron excitation spectra have been computed for large, realistic model systems of the blue copper protein family. Fully quantum-chemical calculations at the density-functional theory level employing polarized triple-味 basis sets have been performed on systems of over 120 atoms, without symmetry. Different mutants, with the ligating methionine of the wild type Cu center exchanged for histidine (M121 H) and glutamine (M121Q), have been investigated in order to obtain insight about how the influence of the exact surrounding milieu of the Cu-atom affects the computed spectrum. With sufficiently large model sizes, inclusion of the environment by using continuum solvation models do not change the spectra significantly. More direct and rigorous treatments are needed to reliably assess the effect of the surrounding protein on the electronic structure of the active sites

The following organizations are acknowledged for financial support: the Ministerio de Ciencia e Innovacion (MICINN, Project Nos. CTQ2008-06532/BQU and CTQ2011-25086/BQU), the DIUE of the Generalitat de Catalunya (project No. 2009SGR528), and the European Fund for Regional Development (FEDER, grant UNGI08-4E-003). M. P. J. was further supported by a MICINN Juan de la Cierva Fellowship (project JCI-2009-05953) and The Academy of Finland (project 136079).

漏 Chemistry and Biodiversity, 2012, vol. 9, n煤m. 9, p. 1728-1738

Wiley

Manager: Ministerio de Ciencia e Innovaci贸n (Espanya)
Ministerio de Educaci贸n y Ciencia (Espanya)
Generalitat de Catalunya. Ag猫ncia de Gesti贸 d鈥橝juts Universitaris i de Recerca
Author: Swart, Marcel
Johansson, Mikael P.
Date: 2012 September 1
Abstract: UV/VIS Electron excitation spectra have been computed for large, realistic model systems of the blue copper protein family. Fully quantum-chemical calculations at the density-functional theory level employing polarized triple-味 basis sets have been performed on systems of over 120 atoms, without symmetry. Different mutants, with the ligating methionine of the wild type Cu center exchanged for histidine (M121 H) and glutamine (M121Q), have been investigated in order to obtain insight about how the influence of the exact surrounding milieu of the Cu-atom affects the computed spectrum. With sufficiently large model sizes, inclusion of the environment by using continuum solvation models do not change the spectra significantly. More direct and rigorous treatments are needed to reliably assess the effect of the surrounding protein on the electronic structure of the active sites
The following organizations are acknowledged for financial support: the Ministerio de Ciencia e Innovacion (MICINN, Project Nos. CTQ2008-06532/BQU and CTQ2011-25086/BQU), the DIUE of the Generalitat de Catalunya (project No. 2009SGR528), and the European Fund for Regional Development (FEDER, grant UNGI08-4E-003). M. P. J. was further supported by a MICINN Juan de la Cierva Fellowship (project JCI-2009-05953) and The Academy of Finland (project 136079).
Format: application/pdf
Citation: 016714
ISSN: 1612-1872 (versi贸 paper)
1612-1880 (versi贸 electr貌nica)
Document access: http://hdl.handle.net/10256/11453
Language: eng
Publisher: Wiley
Collection: MICINN/PN 2012-2014/CTQ2011-25086
MEC/PN 2009-2011/CTQ2008-06532/BQU
AGAUR/2009-2014/2009 SGR-528
Reproducci贸 digital del document publicat a: http://dx.doi.org/10.1002/cbdv.201200058
Articles publicats (D-Q)
Is part of: 漏 Chemistry and Biodiversity, 2012, vol. 9, n煤m. 9, p. 1728-1738
Rights: Tots els drets reservats
Subject: Funcional de densitat, Teoria del
Density functionals
Qu铆mica de l鈥檈stat excitat
Excited state chemistry
Title: Density functional study on UV/VIS spectra of copper-protein active sites: the effect of mutations
Type: info:eu-repo/semantics/article
Repository: DUGiDocs

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