The Control of the Tautomeric Equilibrium of Isocytosine by Intermolecular Interactions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00495590" target="_blank" >RIV/61388963:_____/18:00495590 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/ejoc.201800506" target="_blank" >http://dx.doi.org/10.1002/ejoc.201800506</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/ejoc.201800506" target="_blank" >10.1002/ejoc.201800506</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The Control of the Tautomeric Equilibrium of Isocytosine by Intermolecular Interactions

Popis výsledku v původním jazyce

Isocytosine has two stable tautomers, which can form a dimer with each other, stabilised by three intermolecular hydrogen bonds similar to those in the guanine-cytosine base pair. Molecules with suitable donor/acceptor hydrogen-bonding patterns can form intermolecular complexes with one or the other isocytosine tautomer. These intermolecular interactions stabilise the selected isocytosine tautomer, leading to an increase of its relative concentration. The integration of the H-1 NMR spectra acquired at various temperatures and concentrations was used for the determination of free-energy changes of the formation of the isocytosine dimer/complex. The experimental free-energy changes contain contributions from the formation of the isocytosine dimer/complex itself and from the rearrangement of the solvation shell. The latter contribution was estimated through a comparison of the experimental free-energy changes with those calculated for the dimer/complex formation at the DFT level. The study demonstrates that the molecular environment can change relative tautomer stabilities, which supports the hypothesis of the involvement of rare nucleobase tautomers in the catalytic function of RNA enzymes.

Název v anglickém jazyce

The Control of the Tautomeric Equilibrium of Isocytosine by Intermolecular Interactions

Popis výsledku anglicky

Isocytosine has two stable tautomers, which can form a dimer with each other, stabilised by three intermolecular hydrogen bonds similar to those in the guanine-cytosine base pair. Molecules with suitable donor/acceptor hydrogen-bonding patterns can form intermolecular complexes with one or the other isocytosine tautomer. These intermolecular interactions stabilise the selected isocytosine tautomer, leading to an increase of its relative concentration. The integration of the H-1 NMR spectra acquired at various temperatures and concentrations was used for the determination of free-energy changes of the formation of the isocytosine dimer/complex. The experimental free-energy changes contain contributions from the formation of the isocytosine dimer/complex itself and from the rearrangement of the solvation shell. The latter contribution was estimated through a comparison of the experimental free-energy changes with those calculated for the dimer/complex formation at the DFT level. The study demonstrates that the molecular environment can change relative tautomer stabilities, which supports the hypothesis of the involvement of rare nucleobase tautomers in the catalytic function of RNA enzymes.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GA18-11851S" target="_blank" >GA18-11851S: Intermolekulární interakce studované pomocí NMR spektroskopie a pokročilých kvantově chemických výpočtů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

European Journal of Organic Chemistry

ISSN

1434-193X

e-ISSN

—

Svazek periodika

2018

Číslo periodika v rámci svazku

37

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

5128-5135

Kód UT WoS článku

000446662900007

EID výsledku v databázi Scopus

2-s2.0-85050518845