Palylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F10%3A00046001" target="_blank" >RIV/00216224:14310/10:00046001 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Palylysine-Catalyzed Hydrogen Evolution at Mercury Electrodes
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ELECTROANALYSIS
ISSN
1040-0397
e-ISSN
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Volume of the periodical
22
Issue of the periodical within the volume
17-18
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
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UT code for WoS article
000281904400020
EID of the result in the Scopus database
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