Open AccessTert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes
Author(s) -
Z Drahota,
Pavla Křiváková,
Z Červinková,
Eva Kmonı́čková,
Halka Lotková,
Otto Kučera,
J Houštěk
Publication year - 2005
Publication title -
physiological research
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.647
H-Index - 70
eISSN - 1802-9973
pISSN - 0862-8408
DOI - 10.33549/physiolres.930578
Subject(s) - digitonin , biochemistry , mitochondrion , enzyme , oxidative phosphorylation , flavoprotein , malate dehydrogenase , respiratory chain , nadh dehydrogenase , glutamate dehydrogenase , succinate dehydrogenase , chemistry , biology , glutamate receptor , mitochondrial dna , receptor , gene
Sensitivity of various mitochondrial enzymes to oxidative damage was tested on isolated rat liver hepatocytes permeabilized by digitonin. In permeabilized hepatocytes normal respiratory control values were obtained and mitochondrial membranes remained intact. Respiratory rates of NADH-dependent (glutamate + malate, palmitylcarnitine + malate) and flavoprotein-dependent (succinate) substrates were determined in hepatocytes exposed for 5 min to 0.5-3 mM tert-butyl hydroperoxide before addition of digitonin. Our data showed that oxidation of NADH-dependent substrates is much more sensitive to oxidative stress than oxidation of flavoprotein-dependent ones, evidently due to the modification of iron-sulfur clusters or SH groups in the NADH dehydrogenase enzyme complex (Complex I).