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- W2070829742 abstract "Abstract Incubation of cytochrome P-450 spin labeled by an isocyanide derivative with K 3 Fe(CN) 6 results in a selective disappearance of the spectral components attributable to the weakly immobilized spin labels in the conventional EPR and ST-EPR spectra. The lineshape of that part of the spin-label spectrum which corresponds to the strongly immobilized spin-label molecules remains unaltered. This selective disappearance of distinct parts in complex spectra is important for the analysis and interpretation of ST-EPR spectra from which rotational correlation times are derived. Its applicability is demonstrated for the hepatic membrane-bound cytochrome P-450 of the endoplasmic reticulum, for which the mobility of the spin-labeled isocyanide derivative bound to the active site of the enzyme was determined." @default.
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- W2070829742 date "1982-05-01" @default.
- W2070829742 modified "2023-09-27" @default.
- W2070829742 title "Selective removal of spectral components in complex ST-EPR spectra of spin-labeled cytochrome P-450" @default.
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- W2070829742 doi "https://doi.org/10.1016/0022-2364(82)90206-2" @default.
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