Abstract:
:Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was inactivated by peroxynitrite under biologically relevant conditions. The decrease of enzymatic activity followed an exponential function, and the concentration of peroxynitrite needed to inactivate 50% of 7 microM GAPDH (IC50) was 17 microM. Hydroxyl radical scavengers did not protect GAPDH from inactivation, but molecules that react directly with peroxynitrite such as cysteine, glutathione, or methionine and the substrate, glyceraldehyde 3-phosphate, afforded significant protection. Assuming simple competition kinetics between scavengers and the enzyme, we estimated a second-order rate constant of (2.5 +/- 0.5) x 10(5) M-1 s-1 at 25 degreesC and pH 7.4 for the GAPDH tetramer. The loss of enzyme activity was accompanied by protein thiol oxidation (two thiols oxidized per subunit) with only one critical thiol responsible of enzyme inactivation. Indeed, the pH profile of inactivation was consistent with the reaction of GAPDH sulfhydryls (GAPDH-SH) with peroxynitrite. Peroxynitrite-inactivated GAPDH was resistant to arsenite reduction and only 15% recovered by 20 mM dithiothreitol, suggesting that GAPDH-SH has been mainly oxidized to sulfinic or sulfonic acid, with a minor proportion yielding a disulfide. On the other hand, under anaerobic conditions the peroxynitrite precursor, nitric oxide (*NO), only slowly inactivated GAPDH with a rate constant of 11 M-1 s-1. The remarkable reactivity of the critical thiol group in GAPDH (Cys-149) toward peroxynitrite, which is one order of magnitude higher than that of previously studied sulfhydryls, indicate that it may constitute a preferential intracellular target for peroxynitrite.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Souza JM,Radi Rdoi
10.1006/abbi.1998.0932subject
Has Abstractpub_date
1998-12-15 00:00:00pages
187-94issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(98)90932-8journal_volume
360pub_type
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