1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase |
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Authors: | Johannes Melchers Luise Krauth-Siegel Claudia Muhle-Goll |
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Institution: | 1. Biochemie-Zentrum der Universit?t Heidelberg, Im Neuenheimer Feld 504, 69120, Heidelberg, Germany 2. European Molecular Biology Laboratory, Meyerhofstr.1, 69117, Heidelberg, Germany 3. Max-Planck-Institut für medizinische Forschung, Jahnstrasse 29, 69120, Heidelberg, Germany 4. Karlsruhe Institute of Technology, Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany
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Abstract: | The cysteine-homologues of glutathione peroxidases in Trypanosoma brucei catalyze the trypanothione/tryparedoxin-dependent reduction of hydroperoxides. We report the 1H, 13C, and 15N assignment of the oxidized and reduced form of the enzyme by NMR. Major changes between these two forms were only observed
for residues close to the catalytic site. |
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Keywords: | T brucei Peroxidase Tryparedoxin Resonance assignment |
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