Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F13%3A00422414" target="_blank" >RIV/68081707:_____/13:00422414 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00209805:_____/13:#0000425

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.aca.2013.06.014" target="_blank" >http://dx.doi.org/10.1016/j.aca.2013.06.014</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aca.2013.06.014" target="_blank" >10.1016/j.aca.2013.06.014</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Popis výsledku v původním jazyce

It was originally shown [10] that urease retains its enzymatic activity when adsorbed at bare mercury and solid amalgam surfaces. However the opinion later prevailed that, when adsorbed at bare metal electrodes, proteins are irreversibly denatured. Herewe confirm that urease is enzymatically active at a bare solid amalgam surface as found by Santhanam et al., and we show that this enzyme is equally active at a thiol-modified amalgam surface. We also show that it is the reduced form of urease, which isenzymatically active at Hg surfaces. Oxidation of the protein, resulting in formation of disulfide bonds, strongly decreases the enzyme activity. Using constant current chronopotentiometric stripping (CPS) we show that the exposure of surface-attached urease to negative potentials results in the protein unfolding.

Název v anglickém jazyce

Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Popis výsledku anglicky

It was originally shown [10] that urease retains its enzymatic activity when adsorbed at bare mercury and solid amalgam surfaces. However the opinion later prevailed that, when adsorbed at bare metal electrodes, proteins are irreversibly denatured. Herewe confirm that urease is enzymatically active at a bare solid amalgam surface as found by Santhanam et al., and we show that this enzyme is equally active at a thiol-modified amalgam surface. We also show that it is the reduced form of urease, which isenzymatically active at Hg surfaces. Oxidation of the protein, resulting in formation of disulfide bonds, strongly decreases the enzyme activity. Using constant current chronopotentiometric stripping (CPS) we show that the exposure of surface-attached urease to negative potentials results in the protein unfolding.

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Analytica Chimica Acta

ISSN

0003-2670

e-ISSN

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Svazek periodika

789

Číslo periodika v rámci svazku

JUL30

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

41-46

Kód UT WoS článku

000322610600004

EID výsledku v databázi Scopus

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