Computational study of redox active centres of blue copper proteins: a computational DFT study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F08%3A00206389" target="_blank" >RIV/00216208:11320/08:00206389 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Computational study of redox active centres of blue copper proteins: a computational DFT study

Popis výsledku v původním jazyce

Active sites of blue copper proteins in both reduced and oxidized states were studied at the Density Functional Theory (DFT) level. Two families of these redox sites were examined: the Type A centres with methionine ligand as fourth residue and the TypeB with glutamine residue. Constrained and full optimizations were performed on the protein data bank structures in vacuo and in implicit solvent model simulating protein and water environments. It was found that the redox sites do not possess optimum geometries regardless of the oxidation state. The axial Cu-ligand bond elongates/shortens in the fully optimized Cu(I)/Cu(II) complexes. The reduced centres have a tendency to decrease the coordination number, while a trend to form four -equivalent- bonds is preferred in the oxidized centres. Comparison of the full and constrained optimizations also revealed that the A centres exhibit lower relaxation energies.

Název v anglickém jazyce

Computational study of redox active centres of blue copper proteins: a computational DFT study

Popis výsledku anglicky

Active sites of blue copper proteins in both reduced and oxidized states were studied at the Density Functional Theory (DFT) level. Two families of these redox sites were examined: the Type A centres with methionine ligand as fourth residue and the TypeB with glutamine residue. Constrained and full optimizations were performed on the protein data bank structures in vacuo and in implicit solvent model simulating protein and water environments. It was found that the redox sites do not possess optimum geometries regardless of the oxidation state. The axial Cu-ligand bond elongates/shortens in the fully optimized Cu(I)/Cu(II) complexes. The reduced centres have a tendency to decrease the coordination number, while a trend to form four -equivalent- bonds is preferred in the oxidized centres. Comparison of the full and constrained optimizations also revealed that the A centres exhibit lower relaxation energies.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BJ - Termodynamika

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Physics

ISSN

0026-8976

e-ISSN

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Svazek periodika

106

Číslo periodika v rámci svazku

24

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

16

Strana od-do

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Kód UT WoS článku

000263929200009

EID výsledku v databázi Scopus

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