The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.
|Original language||English (US)|
|Number of pages||8|
|Journal||Protein and Peptide Letters|
|State||Published - 1999|
ASJC Scopus subject areas
- Structural Biology