Article
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
Nature - 1 Jan 2000
Nagai K, Luisi B, Shih D, Miyazaki G, Imai K, Poyart C, De Young A, Kwiatkowsky L, Noble R W, Lin S H
Abstract excerpt
The geometries of the Fe-O2 and Fe-CO bonds in myoglobin and haemoglobin differ significantly from those in free porphyrin model compounds. It has been suggested that steric hindrance by Val-E11 and His-E7 and a hydrogen bond between His-E7 and oxygen affect the geometry and electronic state of the Fe-ligand bond, and that these interactions may be important in controlling oxygen affinity. We have produced mutant...
Topics
- Escherichia coli
- Genetic Engineering
- Hemoglobin A
- Hemoglobin, Sickle
- Humans
- Kinetics
- Mutation
- Oxygen
- Oxyhemoglobins
- Protein Conformation