Academy of Sciences of the Czech Republic: KAN400310651 to EP and KJB100040901, M20004090 to VO, MEYS CR ME09038 to EP, MSM0021622415

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Academy of Sciences of the Czech Republic: KAN400310651 to EP and KJB100040901, M20004090 to VO, MEYS CR ME09038 to EP, MSM0021622415

Authors

Publications

Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes

Živanović, Marko; Aleksić, Mara; Ostatna, Veronika; Doneux, Thomas; Paleček, Emil

(Wiley, 2010)

TY  - JOUR
AU  - Živanović, Marko
AU  - Aleksić, Mara
AU  - Ostatna, Veronika
AU  - Doneux, Thomas
AU  - Paleček, Emil
PY  - 2010
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/5494
AB  - Abstract
It has been shown that peptides and proteins produce at nanomolar concentrations a structure-sensitive chronopotentiometric peak H at mercury electrodes, which is due to the catalytic hydrogen evolution reaction (HER).
Herein, we use for the first time poly(amino acids) to obtain information about the role of individual amino acid
residues in the HER. At pH 6 polylysine (polyLys) and polyarginine,tryptophan yield a peak H, in agreement with
their ionization state, while polyglutamic acid gives no catalytic response. PolyLys catalyzes hydrogen evolution in
its adsorbed state. Even at potentials negative to the potential of zero charge, hydrophobic interactions could be involved in polyLys adsorption.
PB  - Wiley
T2  - Electroanalysis
T1  - Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes
VL  - 22
IS  - 17-18
SP  - 2064
EP  - 2070
DO  - 10.1002/elan.201000088
ER  - 
@article{
author = "Živanović, Marko and Aleksić, Mara and Ostatna, Veronika and Doneux, Thomas and Paleček, Emil",
year = "2010",
abstract = "Abstract
It has been shown that peptides and proteins produce at nanomolar concentrations a structure-sensitive chronopotentiometric peak H at mercury electrodes, which is due to the catalytic hydrogen evolution reaction (HER).
Herein, we use for the first time poly(amino acids) to obtain information about the role of individual amino acid
residues in the HER. At pH 6 polylysine (polyLys) and polyarginine,tryptophan yield a peak H, in agreement with
their ionization state, while polyglutamic acid gives no catalytic response. PolyLys catalyzes hydrogen evolution in
its adsorbed state. Even at potentials negative to the potential of zero charge, hydrophobic interactions could be involved in polyLys adsorption.",
publisher = "Wiley",
journal = "Electroanalysis",
title = "Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes",
volume = "22",
number = "17-18",
pages = "2064-2070",
doi = "10.1002/elan.201000088"
}
Živanović, M., Aleksić, M., Ostatna, V., Doneux, T.,& Paleček, E.. (2010). Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes. in Electroanalysis
Wiley., 22(17-18), 2064-2070.
https://doi.org/10.1002/elan.201000088
Živanović M, Aleksić M, Ostatna V, Doneux T, Paleček E. Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes. in Electroanalysis. 2010;22(17-18):2064-2070.
doi:10.1002/elan.201000088 .
Živanović, Marko, Aleksić, Mara, Ostatna, Veronika, Doneux, Thomas, Paleček, Emil, "Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes" in Electroanalysis, 22, no. 17-18 (2010):2064-2070,
https://doi.org/10.1002/elan.201000088 . .
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