@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"
}