TY - JOUR
T1 - The formation of g = 2.49-species of cytochrome P450 in the rat liver by PCB126 oral administration
T2 - Identification of heme axial ligands by EPR spectroscopy
AU - Morita, Hidetoshi
AU - Yoshikawa, Hiroshi
AU - Takizawa, Tatsuya
AU - Shirai, Mitsuyuki
AU - Akahori, Fumiaki
AU - Yoshimura, Tetsuhiko
N1 - Funding Information:
This work was supported by a Grant-in-Aid for a High Tech Research Center Project from the Ministry of Education, Culture, Sports, Science and Technology of Japan. We would like to express our gratitude to Mr. I. Shiraishi for his assistance.
PY - 2006
Y1 - 2006
N2 - Rat livers and microsomes were subjected to electron paramagnetic resonance (EPR) measurements at 77 K. The EPR spectra of the livers from the control group, carbon tetrachloride-, 3-methylcholanthrene-, and 3,3′,4,4′, 5-pentachlorobiphenyl (PCB126)-treated rats exhibited an EPR spectrum at g = 2.40, 2.24, and 1.93, which is characteristic of P450 in a resting state. The liver of the PCB126-treated rats showed an additional distinct EPR spectrum at g = 2.49, 2.26, and 1.87 (g = 2.49-species). The heme environmental structure of g = 2.49-species was identified by crystal field analysis using three EPR g-values of the microsome treated with various chemicals. These results indicated that g = 2.49-species is a hemeprotein with cysteine thiolate at the 5th coordination site, and a nitrogenous ligand at the 6th site.
AB - Rat livers and microsomes were subjected to electron paramagnetic resonance (EPR) measurements at 77 K. The EPR spectra of the livers from the control group, carbon tetrachloride-, 3-methylcholanthrene-, and 3,3′,4,4′, 5-pentachlorobiphenyl (PCB126)-treated rats exhibited an EPR spectrum at g = 2.40, 2.24, and 1.93, which is characteristic of P450 in a resting state. The liver of the PCB126-treated rats showed an additional distinct EPR spectrum at g = 2.49, 2.26, and 1.87 (g = 2.49-species). The heme environmental structure of g = 2.49-species was identified by crystal field analysis using three EPR g-values of the microsome treated with various chemicals. These results indicated that g = 2.49-species is a hemeprotein with cysteine thiolate at the 5th coordination site, and a nitrogenous ligand at the 6th site.
KW - 3,3′,4,4′, 5-pentachlorobiphenyl (PCB126)
KW - Crystal field analysis
KW - Low-spin Fe(III) hemeprotein
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U2 - 10.1271/bbb.60367
DO - 10.1271/bbb.60367
M3 - Article
C2 - 17151463
AN - SCOPUS:33845910439
SN - 0916-8451
VL - 70
SP - 2974
EP - 2981
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 12
ER -