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Modified Gold Electrodes for Electrochemical Studies of the Reaction of Phospholipid Hydroperoxide Glutathione Peroxidase with Glutathione and Glutathione Disulfide
Author(s) -
Lehmann Claudia,
Wollenberger Ulla,
BrigeliusFlohe Regina,
Scheller Frieder W.
Publication year - 2001
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/1521-4109(200104)13:5<364::aid-elan364>3.0.co;2-z
Subject(s) - glutathione , chemistry , glutathione reductase , phospholipid hydroperoxide glutathione peroxidase , glutathione disulfide , gpx3 , gpx4 , glutathione peroxidase , cyclic voltammetry , redox , glutaredoxin , gpx1 , peroxidase , electrochemistry , biochemistry , organic chemistry , enzyme , electrode
Glutathione peroxidases (GPx) catalyze the reduction of hydroperoxides to the corresponding alcohols under consumption of glutathione. Glutathione is oxidized to glutathione disulfide while the enzyme is regenerated. We electrochemically investigated the reaction of phospholipid hydroperoxide glutathione peroxidase (PHGPx) with glutathione and glutathione disulfide at modified electrodes, prepared by self‐assembling of glutathione, mercaptoundecanoic acid or dodecanthiol onto gold electrodes. The modified electrodes were characterized by cyclic voltammetry using the redox compounds [Ru(NH 3 ) 6 ] 2+ and [Fe(CN) 6 ] 4– . Apart from the reaction with hydroperoxides and glutathione, monomeric PHGPx reacted with glutathione disulfide leading to a mixed selenadisulfide. The tetrameric cytosolic GPx did not react. From the results a transhydrogenase activity of PHGPx is discussed.