1H‐NMR study of reduced heme proteins myoglobin and cytochrome P450

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1H‐NMR study of reduced heme proteins myoglobin and cytochrome P450

BANCI, Lucia; BERTINI, Ivano; MARCONI, Simonetta; PIERATTELLI, Roberta

European journal of biochemistry, 1993-Jul-15, Volume: 215, Issue: 2

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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.

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BANCI, Lucia | BERTINI, Ivano | MARCONI, Simonetta | PIERATTELLI, Roberta

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