The Formation of g=2.49-Species of Cytochrome P450 in the Rat Liver by PCB126 Oral Administration: Identification of Heme Axial Ligands by EPR Spectroscopy
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- MORITA Hidetoshi
- School of Veterinary Medicine, Azabu University High-Tech Research Center, Azabu University
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- YOSHIKAWA Hiroshi
- School of Veterinary Medicine, Azabu University
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- TAKIZAWA Tatsuya
- School of Veterinary Medicine, Azabu University High-Tech Research Center, Azabu University
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- SHIRAI Mitsuyuki
- School of Veterinary Medicine, Azabu University High-Tech Research Center, Azabu University
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- AKAHORI Fumiaki
- School of Veterinary Medicine, Azabu University High-Tech Research Center, Azabu University
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- YOSHIMURA Tetsuhiko
- High-Tech Research Center, Azabu University Institute for Life Support Technology, Yamagata Public Corporation for the Development of Industry
Bibliographic Information
- Other Title
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- The Formation of g=2.49-Species of Cytochome P450 in the Rat Liver by PCB126 Oral Administration: Identification of Heme Axial Ligands by EPR Spectroscopy
- Formation of g 2 49 Species of Cytochome P450 in the Rat Liver by PCB126 Oral Administration Identification of Heme Axial Ligands by EPR Spectroscopy
- The Formation of<i>g</i>=2.49-Species of Cytochrome P450 in the Rat Liver by PCB126 Oral Administration: Identification of Heme Axial Ligands by EPR Spectroscopy
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Abstract
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.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (12), 2974-2981, 2006
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206477078656
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- NII Article ID
- 10018523952
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD2sXktVGqsg%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 8596589
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- PubMed
- 17151463
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed