Magnetic properties of an analog compound for cytochrome P-450 Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/gh93h183d

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  • This thesis describes a Mossbauer effect and electron paramagnetic resonance study of iron (III) tetraphenylporphyrinatobenzenethiolate benzene thiol, an analog compound for bacterial cytochrome P-450. The compound is unusual in that it provides a model for the two ferric reaction states of cytochrome P-450. The iron in the model compound exhibits a gradual low spin to high spin transition over the temperature range 77 to 300 K. Mossbauer spectra for several samples shows that the material, as prepared, consists of at least two species. At 4.2 K the Mossbauer pattern consists of a superposition of two low spin quadrupole doublets (ΔE₁. = 0.282 cm/sec, δ₁ = 0.038 cm/sec, ΔE₁ = 0.175 cm/sec, δ₂ = 0.053 cm/sec). The quadrupole splitting, ΔE₂, of the first component was broadened by paramagnetic hyperfine structure and has been described here by a model relaxation calculation. The EPR spectra at 4.2 K for the two low spin components were similar and could not be resolved from data for polycrystalline samples. The g tensor at 4.2 K is 2.363, 2.240, 1.965. As temperature is increased both these low spin components interconvert to a high spin species with Tc,₁ near 120 K and T c,₂ near 225 K. The Mossbauer and EPR data for the model compound are compared with similar data for the bacterial cytochrome P450 as reported by Gunsalas and co-workers. The data presented here are consistent with the results from other model compounds that contain sulfur as one of the axial ligands and which indicate probable sulfur ligation in the low spin ferric reaction state of cytochrome P450.
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