A 13C‐NMR study of mutant hemoglobins with altered oxygen affinity

FEBS Letters

Norden, Bo²  Smith, Michael L.²  Paul, Karl-Gustav²  Rosa, Jean¹  Edlund, Ulf²  Romeo, Paul-Henry¹ 

[1] Unité de Recherches sur les Anemies, Institut National de la Sante et de la Recherche Medicale U91, Hopital Henri Mondor, 94010 Creteil, France;Departments of Physiological and Organic Chemistry, Umeå University, S-901 87 Umeå, Sweden

关键词: Hemoglobin;    Carbon monoxide;    NMR;    Point mutation;    Protein cooperativity;    Hb A;    normal hemoglobin Ao;    HbHD;    hemoglobin Hôtel Dieu;    HbK;    hemoglobin Kansas;    HbMö;    hemoglobin Malmö;    HbSM;    hemoglobin Saint Mandé;    Mb;    myoglobin;    δ;    chemical shift in ppm from internal DSS;   

DOI  :  10.1016/0014-5793(86)80713-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ¹³CO-NMR spectra of carbonylhemoglobins Saint Mandé (β 102Asn → Tyr), Malmö (β 97His → Gln), Hôtel Dieu (β 99Asp → Gly) and A_o have been determined. The positions of the ¹³CO resonances for hemoglobins A_o, Malmö and Hôtel Dieu were similar indicating similar ligand environments for all. The ¹³CO resonance for the β-subunit of Saint Mandé was upfield-shifted compared to the others. This is evidence that structural changes at the β 102 position directly affect iron-ligand bonding as well as quaternary structure.

【 授权许可】

Unknown