Abstract
X-irradiation of the ternary complex of P450:substrate:O 2 at 77 K produces a reduced intermediate by electron addition to the Fe:O 2 complex which can be studied by EPR-spectroscopy. The EPR spectrum of the new species exhibits rhombic symmetry with g-factors of 2.27, 2.17 and 1.95, respectively. Increasing the temperature of the sample to 190 K results in loss of intensity of the intermediate signals. X-irradiation of oxymyo- and oxyhemoglobin produces similar EPR signals indicating that the added electron is resident on the Fe:O 2 complex (Kappl, R., et al. (1985) Biochim. Biophys. Acta 870, 20–30).
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