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Analysis of Redox Activity of Proteins on the Carbon Screen Printed Electrodes
Author(s) -
Suprun Elena V.,
Zharkova Maria S.,
Morozevich Galina E.,
Veselovsky Alexander V.,
Shumyantseva Victoria V.,
Archakov Alexander I.
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.201300248
Subject(s) - redox , tyrosine , chemistry , electrochemistry , tryptophan , cysteine , electrode , amino acid , inorganic chemistry , combinatorial chemistry , biochemistry , enzyme
Direct redox activity of different proteins was investigated on the surface of carbon screen printed electrodes (SPE). The signal attributed to the electrochemical oxidation of amino acid residues (cysteine (Cys), tryptophan (Trp) and tyrosine (Tyr)) was registered at E max from 0.6 to 0.7 V (vs. Ag/AgCl). Based on the difference in the redox behavior of L ‐tyrosine and 3‐nitro‐ L ‐tyrosine, the selective electrochemical detection of native and nitrated albumins was demonstrated. It was shown that the electrochemical signal correlated with the surface density of electroactive amino acid residues on the protein molecule. A simple electrochemical method for the total protein analysis was proposed.