Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state

被引:41
作者
Paoli, M
Dodson, G
Liddington, RC
Wilkinson, AJ
机构
[1] UNIV YORK, DEPT CHEM, YORK YO1 5DD, N YORKSHIRE, ENGLAND
[2] UNIV LEICESTER, DEPT BIOCHEM, LEICESTER LE1 7RH, LEICS, ENGLAND
基金
英国生物技术与生命科学研究理事会; 英国医学研究理事会;
关键词
haemoglobin; co-operativity; tension; cyanide;
D O I
10.1006/jmbi.1997.1180
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
In 1972, Perutz proposed that the low affinity of T-state haemoglobin is caused by tension in the bond between the iron and the proximal histidine, restraining the Fe from moving into the porphyrin plane on binding oxygen. This proposal has often been disputed. If such tension does exist, it will be manifest in the liganded T-state. Here we describe the structure of the fully liganded T-state cyanide complex of haemoglobin, in which the Fe-proximal histidine bond in the alpha-subunits, but not in the beta-subunits, is ruptured. This rupture uncouples the structural changes at the alpha-haem from those in the globin and the beta-haem, and demonstrates unequivocally the existence of tension and its transmission through this bond. (C) 1997 Academic Press Limited.
引用
收藏
页码:161 / 167
页数:7
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