Magnetic circular dichroism studies of hepatic microsomal cytochrome P-450.

Biochemistry
T ShimizuR Sato

Abstract

Magnetic circular dichroism (MCD) spectra have been measured for cytochrome P-450 (P-450) purified from phenobarbital-induced rabbit liver microsomes. The temperature dependence of some of the MCD spectra has also been determined. The MCD spectrum of oxidized P-450 seems to suggest that it is in a state intermediate between the ferric low-spin states. Model experiments suggest that this anomaly arises from the coordination of a thiolate anion to the heme. Reduced P-450 shows a very peculiar MCD spectrum; the spectrum as well as its temperature dependence suggest that the heme in reduced P-450 is a "mixture" in terms of redox and/or spin states. The MCD spectrum of the CO complex of reduced P-450 exhibits an apparent Faraday A term around 450 nm which consists of about 50% C term and 50% the other terms, indicating that it is not in a purely ferrous low-spin state. The CO complex of reduced cytochrome P-420 (P-420), on the other hand, shows an MCD spectrum characteristic of a ferrous low-spin heme. It is suggested from model experiments that the thiolate anion coordinates to the heme trans to CO in the P-450-CO complex. The Soret region of the MCD spectrum of the EtNC complex of reduced P-450 is characterized by two apparent A t...Continue Reading

References

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Citations

Aug 23, 1977·Biochimica Et Biophysica Acta·N KobayashiM Hatano
Jun 21, 1978·Biochimica Et Biophysica Acta·T NozawaY Ishimura
Apr 25, 1979·Biochimica Et Biophysica Acta·W R Browett, M J Stillman
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Jan 9, 2013·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Daniel W NebertWalter L Miller
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Sep 1, 1997·Archives of Biochemistry and Biophysics·L A AnderssonJ A Peterson
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Aug 31, 2019·The Journal of Biological Chemistry·Leon P JennerMyles R Cheesman
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