对氧亲和力改变的突变血红蛋白的13C核磁共振研究。
A 13C-NMR study of mutant hemoglobins with altered oxygen affinity.
作者信息
Smith M L, Norden B, Edlund U, Romeo P H, Rosa J, Paul K G
出版信息
FEBS Lett. 1986 Jul 7;202(2):337-9. doi: 10.1016/0014-5793(86)80713-x.
The 13CO-NMR spectra of carbonylhemoglobins Saint Mandé (beta 102Asn----Tyr), Malmö (beta 97His----Gln), Hôtel Dieu (beta 99Asp----Gly) and Ao have been determined. The positions of the 13CO resonances for hemoglobins Ao, Malmö and Hôtel Dieu were similar indicating similar ligand environments for all. The 13CO resonance for the beta-subunit of Saint Mandé was upfield-shifted compared to the others. This is evidence that structural changes at the beta 102 position directly affect iron-ligand bonding as well as quaternary structure.
已测定了圣曼德（β102天冬酰胺→酪氨酸）、马尔默（β97组氨酸→谷氨酰胺）、迪厄医院（β99天冬氨酸→甘氨酸）和奥血红蛋白的13C-核磁共振谱。奥、马尔默和迪厄医院血红蛋白的13CO共振位置相似，表明它们的配体环境相似。与其他血红蛋白相比，圣曼德β亚基的13CO共振发生了高场位移。这证明β102位置的结构变化直接影响铁-配体键合以及四级结构。
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