Electron spin resonance studies of wild-type and mutant cytochromes P-450d: effects of mutations at proximal, aromatic and distal sites on g values.

Sotokawa, H; Shimizu, T; Furuya, H; Sadeque, A J; Hatano, M; Ohba, Y; Iwaizumi, M; Fujii-Kuriyama, Y

Sotokawa, H; Shimizu, T; Furuya, H; Sadeque, A J; Hatano, M; Ohba, Y; Iwaizumi, M; Fujii-Kuriyama, Y.

Affiliation

Sotokawa H; Chemical Research Institute of Nonaqueous Solutions, Tohoku University, Katahira, Japan.

Biochim Biophys Acta ; 1037(1): 122-8, 1990 Jan 19.

Article in En | MEDLINE | ID: mdl-2153026

Subject(s)

Cytochrome P-450 Enzyme System; Animals; Carbon Monoxide; Cytochrome P-450 Enzyme System/genetics; DNA Mutational Analysis; Electron Spin Resonance Spectroscopy; Heme; Microsomes, Liver/enzymology; Rats; Structure-Activity Relationship

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Collection: 01-internacional Database: MEDLINE Main subject: Cytochrome P-450 Enzyme System Limits: Animals Language: En Journal: Biochim Biophys Acta Year: 1990 Type: Article Affiliation country: Japan

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