Thread: NMR paper 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
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Default 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.

Related Articles 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.

Eur J Biochem. 1993 Jul 15;215(2):431-7

Authors: Banci L, Bertini I, Marconi S, Pierattelli R

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.

PMID: 8344310 [PubMed - indexed for MEDLINE]



Source: PubMed
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