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• W2077689694 abstract "Rotational diffusion of cytochrome P-450 in rabbit liver microsomes has been studied by saturation transfer EPR spectroscopy. Sulfhydryl groups of cytochrome P-450 were selectively modified using a maleimide spin label. The effective rotational correlation time for the rotation of cytochrome P-450 was calculated to be about 480 μs which corresponds to a very strong immobilization thus evidencing protein aggregation within the membrane. The anisotropic character of the spectra indicates a nonspherical shape and/or anisotropic rotational motion of the cluster. The temperature dependence of the rotational correlation time shows a relatively sharp break at about 4 °C but only small changes above this temperature. The break at about 4 °C is probably caused by the onset of the cluster rotation. Below 4 °C the enzyme is almost immobilized. A similar complete immobilization can be achieved by treating the microsomes with glutaraldehyde." @default.
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• W2077689694 date "1982-06-01" @default.
• W2077689694 modified "2023-10-16" @default.
• W2077689694 title "Rotational diffusion of cytochrome P-450 in the microsomal membrane—Evidence for a clusterlike organization from saturation transfer electron paramagnetic resonance spectroscopy" @default.
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• W2077689694 doi "https://doi.org/10.1016/0003-9861(82)90217-x" @default.
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