Very high-field EPR study of glycyl radical enzymes
| Autor: | Etienne Mulliez, Alia K. Hassan, Johann Heider, Marc Fontecave, Carole Duboc-Toia, Christina Leutwein, Sandrine Ollagnier de Choudens |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
biology Free Radicals Stereochemistry Radical Electron Spin Resonance Spectroscopy Glycine General Chemistry Anaerobic ribonucleotide reductase Biochemistry Complete resolution Catalysis law.invention Colloid and Surface Chemistry Enzyme chemistry law Pyruvate formate lyase Benzylsuccinate synthase Ribonucleotide Reductases biology.protein Anisotropy High field Electron paramagnetic resonance |
| Zdroj: | Journal of the American Chemical Society. 125(1) |
| ISSN: | 0002-7863 |
| Popis: | This work shows that very high-field EPR spectroscopy allows a rather accurate determination of the g-tensor of protein radicals, including C-centered ones, and thus may be used as a probe for distinguishing a tyrosyl-, a glycyl-, or a tryptophanyl-radical. In this paper, we report the first complete analysis of the g-tensor of glycyl radical enzymes (anaerobic ribonucleotide reductase, pyruvate formate lyase, and benzylsuccinate synthase), thus providing new information on their EPR properties. Because the g-anisotropy is small, the complete resolution of the g-tensor could be only obtained at very high field (18.8 T). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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