H-1-NMR STUDY OF REDUCED HEME-PROTEINS MYOGLOBIN AND CYTOCHROME-P450

被引：18

作者：

BANCI, L ^{[1
]}

BERTINI, I ^{[1
]}

MARCONI, S ^{[1
]}

PIERATTELLI, R ^{[1
]}

机构：

[1] UNIV FLORENCE, DEPT CHEM, VIA G CAPPONI 7, I-50121 FLORENCE, ITALY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 215卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1993.tb18050.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The H-1-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 deoxy-myoglobin. 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.

引用

页码：431 / 437

页数：7

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