Article
Mutational effects at the subunit interfaces of human hemoglobin: evidence for a unique sensitivity of the T quaternary state to changes in the hinge region of the alpha 1 beta 2 interface.
Biochemistry - 16 Oct 2001
Noble R W, Hui H L, Kwiatkowski L D, Paily P, DeYoung A, Wierzba A, Colby J E, Bruno S, Mozzarelli A
Abstract excerpt
A set of variant human hemoglobins, each with an Ala or Gly substitution at a single residue, has been prepared, and the kinetics of their reactions with carbon monoxide have been measured. This reaction is rate-limited by the binding of the first CO to the deoxygenated T state of the protein. Th...
Topics
- Amino Acid Substitution
- Carbon Monoxide
- Dimerization
- Globins
- Hemoglobin A
- Hemoglobins
- Humans
- In Vitro Techniques
- Iron
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Oxygen