1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase.
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.
Melchers
Johannes
J
Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 504, 69120 Heidelberg, Germany.
Krauth-Siegel
Luise
L
Muhle-Goll
Claudia
C
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes / Q000737:chemistry; D005979:Glutathione Peroxidase / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry*; D011522:Protons; D015800:Protozoan Proteins / Q000737:chemistry*; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D015800:Protozoan Proteins; D010544:Peroxidases; C110959:tryparedoxin peroxidase; D005979:Glutathione Peroxidase