EPR-spectroscopy of reduced oxyferrous-P450cam.
X-irradiation of the ternary complex of P450:substrate:O2 at 77 K produces a reduced intermediate by electron addition to the Fe:O2 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:O2 compleX (Kappl, R., et al. (1985) Biochim. Biophys. Acta 870, 20-30).
Davydov
R
R
Fachrichtung Biophysik und Physikalische Grundlagen, Medizin Universität des Saarlandes, Homburg/Saar, Germany.
Kappl
R
R
Hüttermann
J
J
Peterson
J A
JA
D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D014965:X-Rays
D005609:Free Radicals; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase