Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes
Original language description
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.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Result continuities
Project
<a href="/en/project/GA18-18154S" target="_blank" >GA18-18154S: New tools of label-free electrochemical analysis of protein interactions with nucleic acids and proteins</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ChemPlusChem
ISSN
2192-6506
e-ISSN
—
Volume of the periodical
85
Issue of the periodical within the volume
7
Country of publishing house
DE - GERMANY
Number of pages
6
Pages from-to
1596-1601
UT code for WoS article
000555737600027
EID of the result in the Scopus database
2-s2.0-85088821654