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EPR‐spectroscopy of reduced oxyferrous‐P450 cam
Author(s) -
Davydov R.,
Kappl R.,
Hüttermann J.,
Peterson J.A.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81398-r
Subject(s) - electron paramagnetic resonance , spectroscopy , chemistry , nuclear magnetic resonance , physics , quantum mechanics
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).