Polylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes
| Autor: | Marko N. Živanović, Emil Paleček, Mara M. Aleksić, Thomas Doneux, Veronika Ostatná |
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| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Chemistry Polyglutamic acid Inorganic chemistry chemistry.chemical_element 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Analytical Chemistry Catalysis Amino acid Mercury (element) Hydrophobic effect chemistry.chemical_compound Adsorption Hanging mercury drop electrode Polylysine Electrochemistry 0210 nano-technology |
| Zdroj: | Electroanalysis. 22:2064-2070 |
| ISSN: | 1040-0397 |
| DOI: | 10.1002/elan.201000088 |
| 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. |
| Databáze: | OpenAIRE |
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