Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes

0539351 - BFÚ 2021 RIV DE eng J - Článek v odborném periodiku
Dorčák, Vlastimil - Černocká, Hana - Paleček, Emil
Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes.
ChemPlusChem. Roč. 85, č. 7 (2020), s. 1596-1601. ISSN 2192-6506. E-ISSN 2192-6506
Grant CEP: GA ČR(CZ) GA18-18154S
Institucionální podpora: RVO:68081707
Klíčová slova: electrochemical analysis * mass-spectrometry * heavy-water * exchange * stability * proteins
Obor OECD: Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Impakt faktor: 2.863, rok: 2020
Způsob publikování: Omezený přístup
https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000348

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.
Trvalý link: http://hdl.handle.net/11104/0317041