EPR‐spectroscopy of reduced oxyferrous‐P450cam
- 16 December 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 295 (1-3) , 113-115
- https://doi.org/10.1016/0014-5793(91)81398-r
Abstract
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).Keywords
This publication has 9 references indexed in Scilit:
- One-electron reduction of the oxy form of cobalt-substituted hemoproteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin.Journal of Biological Chemistry, 1988
- One-electron reduction of the oxyform of 2,4-diacetyldeuterocytochrome P-450cam.Journal of Biological Chemistry, 1987
- Spin-density distribution in the [FeO2]− complex. Electron spin resonance of myoglobin single crystalsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Electron spin and electron nuclear double resonance of the [FeO2]− centre from irradiated oxyhemo- and oxymyoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- One-electron reduction in oxyform of hemoproteins.Journal of Biological Chemistry, 1981
- Cytochrome P-450: Biophysical Properties and Catalytic FunctionPublished by Elsevier ,1979
- [15] Purification of bacterial cytochrome P-450Published by Elsevier ,1978
- Pseudomonas putida cytochrome P-450: Characterization of an oxygenated form of the hemoproteinArchives of Biochemistry and Biophysics, 1972