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- W2327571410 abstract "The model system consisting of α-mercaptopropionylglycine (α-MPG), hemin and pyridine exhibited similar absorption and electron paramagnetic resonance spectra to cytochrome P-450. In the presence of an excess amount of pyridine, a low-spin state of heme iron was observed at both 293 and 77°K. A transition of the high-spin state of Fe (III) at 293°K to the low-spin state was detected at 77°K in the presence of trace amount of pyridine. When pyridine was omitted from the system, the high-spin state was produced. Under exposure of CO of this model system, the characteristic absorption band of 450 nm was observed, which is typical with cytochrome P-450. Two types of spectral change were obtained when aminopyrine (type I) or aniline (type II) was added to α-MPG-hemin. Spectral dissociation constant Ks of aniline with model system was compared with the reported value with a biological system. It was also discussed that the hydroxylating ability with model and liver microsomal systems." @default.
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- W2327571410 date "1978-01-01" @default.
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- W2327571410 title "A model of cytochrome P-450; optical and EPR properties of a thiol-containing peptide-hemin system and its activity of aniline hydroxylation." @default.
- W2327571410 doi "https://doi.org/10.1248/cpb.26.1348" @default.
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