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Palylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes

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ZIVANOVIC Marko ALEKSIC Mara OSTATNA Veronika DONEUX Thomas PALEČEK Emil

Rok publikování 2010
Druh Článek v odborném periodiku
Časopis / Zdroj ELECTROANALYSIS
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Obor Biofyzika
Klíčová slova Catalytic hydrogen evolution; Constant current chronopotentiometric stripping; Hanging mercury drop electrode; Poly(amino acids); Polylysine; Amino acids
Popis 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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