Effects of mutations on the absorption spectra of copper proteins: a QM/MM study

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Abstract

The ground and excited state properties of copper proteins are studied and analyzed using hybrid quantum mechanics/molecular mechanics technique. Wild-type plastocyanin, characterized by an intense blue color, and wild-type nitrosocyanin, a red protein, are considered. These proteins differ from some ligands of the copper containing chromophore; we also studied the effects of selective mutations of one of the active site residue in plastocyanin. It is shown that this mutation is able to strongly modify the UV/VIS spectrum continuously modifying the absorption spectrum of the protein that from blue becomes red. Electrostatic and polarization effects of the macromolecular environment on the chromophore are taken into account using original techniques. Principal transitions are analyzed by mean of natural transition orbitals.

Keywords

QM/MM TD-DFT Absorption spectra Copper protein 
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Notes

Acknowledgments

Supports from Université de Lorraine and CNRS are gratefully acknowledged, also for the financing of the “chaire d’excellence” (A. M.). We also acknowledge support from the ANR project ANR-09-BLAN-0191-01 “PhotoBioMet”.

Supplementary material

214_2012_1221_MOESM1_ESM.docx (16 kb)
Supplementary material 1 (DOCX 16 kb)

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Copyright information

© Springer-Verlag 2012

Authors and Affiliations

  1. 1.Equipe de Chimie et Biochime Théoriques, SRSMC-UMR 7565Université de Lorraine-Nancy and CNRSNancy-VandoeuvreFrance

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