Peroxidation of a Specific Tryptophan of Metmyoglobin by Hydrogen Peroxide
| Autor: | Richard A. Tschirret-Guth, Ronald P. Mason, Janice A. DeGray, Michael R. Gunther, Paul R. Ortiz de Montellano |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Indole test
Free Radicals Protein Conformation Chemistry Radical Electron Spin Resonance Spectroscopy Tryptophan Whales Hydrogen Peroxide Cell Biology Crystallography X-Ray Biochemistry chemistry.chemical_compound Metmyoglobin Myoglobin Mutagenesis Site-Directed Animals Tyrosine Hydrogen peroxide Molecular Biology Histidine |
| Zdroj: | Journal of Biological Chemistry. 272:2359-2362 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.4.2359 |
| Popis: | Globin-centered radicals at tyrosine and tryptophan residues and a peroxyl radical at an unknown location have been reported previously as products of the reaction of metmyoglobin with hydrogen peroxide. The peroxyl radical is shown here to be localized on tryptophan through the use of recombinant sperm whale myoglobin labeled with 13C at the indole ring C-3. Peroxyl radical formation was not prevented by site-directed mutations that replaced all three tyrosines, the distal histidine, or tryptophan 7 with non-oxidizable residues. In contrast, mutation of tryptophan 14 prevents peroxyl radical formation, implicating tryptophan 14 as the specific site of the peroxidation. |
| Databáze: | OpenAIRE |
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