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|Title:||Lineshape analysis of heme-protein-derived radicals based on simulation of EPR spectra||Authors:||Pogni, Rebecca
DELLA LUNGA, G
|Keywords:||EPR; computer simulation; heme proteins; H2O2; spin trap||Issue Date:||1999||Project:||None||Journal:||INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY||Abstract:||
The reaction of heme proteins and H2O2 is thought to proceed viatwo-electron oxidation, resulting in the formation of ferryl heme FeIVsO., and aprotein radical. The ferryl-radical form of heme proteins would then catalyze theoxidation of molecules. Incubation of heme proteins with H2O2 in the presence ofmethyl-nitrosopropane MNP. resulted in the detection of electron paramagneticresonance EPR. spectra characteristic of a highly immobilized nitroxide. Lineshapes ofthe EPR spectra were consistent with a slow tumbling molecule as it is evident from thebroadening of the high field lines. This is consistent with the high molecular mass of theradical adduct. The goal of this work is, using a computer program based on thestochastic Liouville equation, to simulate directly these slow-motional EPR spectra andobtain information on magnetic and dynamic parameters of the complexes.
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