Reorganisation Energy for Internal Electron Transfer in Multicopper Oxidases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F11%3A00367566" target="_blank" >RIV/61388963:_____/11:00367566 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jp205897z" target="_blank" >http://dx.doi.org/10.1021/jp205897z</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp205897z" target="_blank" >10.1021/jp205897z</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Reorganisation Energy for Internal Electron Transfer in Multicopper Oxidases

Popis výsledku v původním jazyce

We have calculated the reorganization energy for the intramolecular electron transfer between the reduced type 1 copper site and the peroxy intermediate of the trinuclear cluster in the multicopper oxidase CueO. The calculations are performed at the combined quantum mechanics and molecular mechanics (QM/MM) level, based on molecular dynamics simulations with tailored potentials for the two copper sites. We obtain a reorganization energy of 91-133 kJ/mol, depending on the theoretical treatment. The two Cu sites contribute by 12 and 22 kJ/mol to this energy, whereas the solvent contribution is 34 kJ/mol. The rest comes from the protein, involving small contributions from many residues. We have also estimated the energy difference between the two electron-transfer states and show that the reduction of the peroxy intermediate is exergonic by 43-87 kJ/mol, depending on the theoretical method.

Název v anglickém jazyce

Reorganisation Energy for Internal Electron Transfer in Multicopper Oxidases

Popis výsledku anglicky

We have calculated the reorganization energy for the intramolecular electron transfer between the reduced type 1 copper site and the peroxy intermediate of the trinuclear cluster in the multicopper oxidase CueO. The calculations are performed at the combined quantum mechanics and molecular mechanics (QM/MM) level, based on molecular dynamics simulations with tailored potentials for the two copper sites. We obtain a reorganization energy of 91-133 kJ/mol, depending on the theoretical treatment. The two Cu sites contribute by 12 and 22 kJ/mol to this energy, whereas the solvent contribution is 34 kJ/mol. The rest comes from the protein, involving small contributions from many residues. We have also estimated the energy difference between the two electron-transfer states and show that the reduction of the peroxy intermediate is exergonic by 43-87 kJ/mol, depending on the theoretical method.

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/LC512" target="_blank" >LC512: Centrum biomolekul a komplexních molekulových systémů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

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Svazek periodika

115

Číslo periodika v rámci svazku

45

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

16

Strana od-do

13111-13126

Kód UT WoS článku

000296686000001

EID výsledku v databázi Scopus

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