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Catalysis of Hydrogen Evolution by Polylysine, Polyarginine and Polyhistidine at Mercury Electrodes
Author(s) -
Vargová Veronika,
Zivanović Marko,
Dorčák Vlastimil,
Paleček Emil,
Ostatná Veronika
Publication year - 2013
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.201300170
Subject(s) - polylysine , histidine , chemistry , amino acid , lysine , catalysis , macromolecule , cyclic voltammetry , combinatorial chemistry , electrode , biophysics , biochemistry , electrochemistry , biology
Protein catalyzed hydrogen evolution reaction at mercury‐containing electrodes controlled by constant‐current chronopotentiometric stripping (CPS) is representing a new tool useful in protein research. The resulting CPS peak H is sensitive to changes in the protein structure and its amino acid composition. Besides CPS, cyclic voltammetry appears to be useful for study of poly(amino acids) as an intermediate model system between peptides and macromolecular proteins. Here we show that similarly as arginine in polyarginine and lysine in polylysine also histidine residues in polyhistidine contribute to the catalysis of hydrogen evolution under the given conditions. Peak potentials of individual poly(amino acids) are different and depend on the type of amino acid residues.