EPR-SPECTROSCOPY OF REDUCED OXYFERROUS-P450CAM

被引：63

作者：

DAVYDOV, R

KAPPL, R

HUTTERMANN, J

PETERSON, JA

机构：

[1] UNIV SAARLAND,FACHRICHTUNG BIOPHYS & PHYS GRUNDLAGEN MED,KLINIKUM BAU 76,W-6650 HOMBURG,GERMANY

[2] UNIV TEXAS,SW MED CTR,DEPT BIOCHEM,DALLAS,TX 75235

来源：

FEBS LETTERS | 1991年 / 295卷 / 1-3期

关键词：

CYTOCHROME P450; OXYGEN ACTIVATION; EPR-SPECTROSCOPY; ONE-ELECTRON REDUCTION; HEME-OXYGEN COMPLEX;

D O I：

10.1016/0014-5793(91)81398-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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).

引用

页码：113 / 115

页数：3

共 9 条

[1]

BREWER CB, 1988, J BIOL CHEM, V263, P791

[2]

Griffin B. W., 1979, PORPHYRINS, V7, P333

[3] ELECTRON-SPIN AND ELECTRON NUCLEAR DOUBLE-RESONANCE OF THE [FEO2]- CENTER FROM IRRADIATED OXYHEMOGLOBIN AND OXYMYOGLOBIN [J].