Effect of Protein Microenvironment on Tyrosyl Radicals. A High-Field (285 GHz) EPR, Resonance Raman, and Hybrid Density Functional Study
| Autor: | Tony A. Mattioli,†,§ and, Sun Un, Anabella Ivancich |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Field (physics)
Radical Infrared spectroscopy Resonance General Chemistry Biochemistry Catalysis law.invention chemistry.chemical_compound symbols.namesake Colloid and Surface Chemistry chemistry Computational chemistry law symbols Physical chemistry Molecular orbital Raman spectroscopy Electron paramagnetic resonance Heme |
| Zdroj: | Journal of the American Chemical Society. 121:5743-5753 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja990562m |
| Popis: | The protein environment appears to regulate the biological function of tyrosyl radicals (Tommos, C.; Babcock, G. T. Acc. Chem. Res. 1998, 31, 18−25). Vibrational spectroscopy and electron paramagnetic resonance (EPR) techniques have been used to characterize tyrosyl radicals. In this work, we have investigated the relationship between the g values and the vibrational spectra of tyrosyl radicals (Tyr•) in different protein microenvironments by combining experimentally determined values and molecular orbital calculations. High-field (285 GHz) electron paramagnetic resonance (HF-EPR) and resonance Raman spectroscopies were applied to obtain the g values and the vibrational frequencies, respectively, of the tyrosyl radical (Tyr•CAT) previously reported as a heme catalase intermediate [(Fe(IV)O) Tyr•] (Ivancich, A.; Jouve, H. M.; Gaillard, J. J. Am. Chem. Soc. 1996, 118, 12852−12853. Ivancich, A., Jouve, H. M.; Sartor, B.; Gaillard, J. Biochemistry 1997, 36, 9356−9364). The effect of the protein microenvironme... |
| Databáze: | OpenAIRE |
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