Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6374
Title: In silico spectroscopy of tryptophan and tyrosine radicals involved in the long-range electron transfer of Cytochrome c Peroxidase
Authors: Bernini, Caterina
Arezzini, E.
Basosi, Riccardo 
Sinicropi, Adalgisa 
Issue Date: 2014
Project: None 
Journal: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Abstract: 
Cytochrome c peroxidase (CcP) is a heme-containing enzyme that catalyzesthe oxidation of the ferrocytochrome c to ferricytochrome c with concomitant reduction ofH2O2 to H2O. Its catalytic cycle involves the formation of a double oxidized species(compound I) consisting of an oxoferryl center (Fe(IV)=O) and an amino acid radical(R•). Here we use a quantum-mechanics/molecular-mechanics (QM/MM) computationalprotocol based on density functional theory (DFT) and multiconfigurational perturbationtheory (CASPT2) methods to reproduce specific features of compound I EPR and UV−visspectra. The results show that the employed QM/MM models can correctly predict themagnetic, electronic and vibrational properties of the observed amino acid radicals ofcompound I. Furthermore, we have been able to confirm that the principal radical species ofcompound I is a tryptophan cationic radical located on residue 191 (Trp191•+) and thatthree tyrosine residues (Tyr203, Tyr236, and Tyr251), located along two possible ET pathways involving Trp191•+, are possiblecandidates to host the secondary radical species.
Description: 
60877
URI: http://hdl.handle.net/20.500.12779/6374
ISSN: 1520-6106
DOI: 10.1021/jp5025153
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