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- W2005010169 abstract "The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the hyperfine-shifted signals of deoxymyoglobin. The nuclear longitudinal-relaxation-time values indicate short electron-relaxation times whereas Curie relaxation contributes significantly to the signals linewidths. For reduced cytochrome P450 the linewidths are larger due to the Curie-relaxation contribution in a large protein. Therefore, the spectral information is poor. The electron-relaxation rates are discussed in terms of possible electronic structure." @default.
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- W2005010169 date "1993-07-01" @default.
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- W2005010169 title "1H-NMR study of reduced heme proteins myoglobin and cytochrome P450" @default.
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- W2005010169 doi "https://doi.org/10.1111/j.1432-1033.1993.tb18050.x" @default.
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