Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F20%3A00539351" target="_blank" >RIV/68081707:_____/20:00539351 - isvavai.cz</a>

Výsledek na webu

<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000348" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000348</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cplu.202000348" target="_blank" >10.1002/cplu.202000348</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes

Popis výsledku v původním jazyce

The hydrogen evolution reaction (HER), catalysed by proteins at mercury electrodes and reflected in chronopotentiometric stripping peak H, provides a label-free and reagentless analytical technique that is sensitive to protein structure. Here we show how the kinetic isotope effect affected the HER catalysed by the protein bovine serum albumin (BSA). We found that the deuteron bond, which is stronger than that of a proton, contributed to less effective transport of deuterons mediated by BSA at the Hg|D2O interface, and enhanced structural stability of the surface-attached native BSA in D2O solution. A structural transition was also observed in the surface-attached urea-denatured BSA, and is probably due to the destabilisation of some secondary structural remnants retained by the 17 SS-bonds. Because the catalytically active groups involved in proton or deuteron transfer in native proteins are often exposed towards solutions and their protons exchange almost instantly, no signs of H/D exchange were observed in native BSA using peak H under the given conditions.

Název v anglickém jazyce

Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes

Popis výsledku anglicky

The hydrogen evolution reaction (HER), catalysed by proteins at mercury electrodes and reflected in chronopotentiometric stripping peak H, provides a label-free and reagentless analytical technique that is sensitive to protein structure. Here we show how the kinetic isotope effect affected the HER catalysed by the protein bovine serum albumin (BSA). We found that the deuteron bond, which is stronger than that of a proton, contributed to less effective transport of deuterons mediated by BSA at the Hg|D2O interface, and enhanced structural stability of the surface-attached native BSA in D2O solution. A structural transition was also observed in the surface-attached urea-denatured BSA, and is probably due to the destabilisation of some secondary structural remnants retained by the 17 SS-bonds. Because the catalytically active groups involved in proton or deuteron transfer in native proteins are often exposed towards solutions and their protons exchange almost instantly, no signs of H/D exchange were observed in native BSA using peak H under the given conditions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Projekt

<a href="/cs/project/GA18-18154S" target="_blank" >GA18-18154S: Nové nástroje elektrochemické analýzy proteinových interakcí s nukleovými kyselinami a proteiny nevyžadující značení</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

ChemPlusChem

ISSN

2192-6506

e-ISSN

—

Svazek periodika

85

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

6

Strana od-do

1596-1601

Kód UT WoS článku

000555737600027

EID výsledku v databázi Scopus

2-s2.0-85088821654