Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8300940 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2018 | 49 Pages |
Abstract
At lower H2O2 levels (100 μM), GSTU23 forms methionine sulfoxides. Specifically, oxidation of Met14, located near the catalytic Ser13, could interfere with both GSH binding and catalytic activation. At higher H2O2 levels (200 μM), the Cys65-Cys110 disulfide bond protects other cysteines and also methionines from overoxidation. This study shows the impact of oxidative stress on GSTU23 regulated by methionine sulfoxide reductases and glutaredoxin, and the mechanisms involved in maintaining its catalytic functionality under oxidizing conditions.
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Authors
Maria-Armineh Tossounian, Inge Van Molle, Khadija Wahni, Silke Jacques, Kris Gevaert, Frank Van Breusegem, Didier Vertommen, David Young, Leonardo Astolfi Rosado, Joris Messens,