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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