P-31-NMR INVESTIGATION OF TRIMETHYLPHOSPHINE BINDING TO [ALPHA-FE(II),BETA-MN(II)] HYBRID HEMOGLOBIN - A MODEL FOR PARTIALLY LIGANDED SPECIES

被引：7

作者：

BONDON, A ^{[1
]}

SIMONNEAUX, G ^{[1
]}

机构：

[1] UNIV RENNES 1,CHIM ORGANOMET LAB,CNRS,UA 415,F-35042 RENNES,FRANCE

来源：

BIOPHYSICAL CHEMISTRY | 1990年 / 37卷 / 1-3期

关键词：

Hemoglobin; Mixed-metal hybrid; Trimethylphosphine binding;

D O I：

10.1016/0301-4622(90)88039-U

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：

31P-NMR of trimethylphosphine binding to the ferrous chains of a ([αFe(II),βMn(II)]hemoglobin hybrid is employed to sinvestigate partially liganded species. This study shows that at low pH (6.5), in the presence of inositol hexaphosphate, the resonance at 23.2 ppm (from H3PO4) is due to phosphine bonding to α-chains in the T quaternary state. At elevated pH (7.6), phosphine binding to the α-chains produces a resonance at 24.8 ppm which is associated with a T-to-R conversion. These findings are discussed in relation with our previous results on direct observation of intermediate ligation states of hemoglobin. © 1990.

引用

页码：407 / 411

页数：5

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