Palylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes

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Authors	ZIVANOVIC Marko ALEKSIC Mara OSTATNA Veronika DONEUX Thomas PALEČEK Emil
Year of publication	2010
Type	Article in Periodical
Magazine / Source	ELECTROANALYSIS
MU Faculty or unit	Faculty of Science
Citation
Field	Biophysics
Keywords	Catalytic hydrogen evolution; Constant current chronopotentiometric stripping; Hanging mercury drop electrode; Poly(amino acids); Polylysine; Amino acids
Description	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.
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