Lineshape analysis of heme-protein-derived radicals based on simulation of EPR spectra
✍ Scribed by Rebecca Pogni; Giovanni Della Lunga; Elena Busi; Riccardo Basosi
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 161 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0020-7608
No coin nor oath required. For personal study only.
✦ Synopsis
The reaction of heme proteins and H O is thought to proceed via 2 2 Ž IV . two-electron oxidation, resulting in the formation of ferryl heme Fe s O , and a protein radical. The ferryl-radical form of heme proteins would then catalyze the oxidation of molecules. Incubation of heme proteins with H O in the presence of 2 2
Ž
. methyl-nitrosopropane MNP resulted in the detection of electron paramagnetic Ž . resonance EPR spectra characteristic of a highly immobilized nitroxide. Lineshapes of the EPR spectra were consistent with a slow tumbling molecule as it is evident from the broadening of the high field lines. This is consistent with the high molecular mass of the radical adduct. The goal of this work is, using a computer program based on the stochastic Liouville equation, to simulate directly these slow-motional EPR spectra and obtain information on magnetic and dynamic parameters of the complexes.