Abstract
A hypothesis about the evolution of the haem-haem interaction in haemoglobins has been formulated on the basis of available functional and structural data. It emerges that this cooperative mechanism is not necessarily due solely to the higher levels of protomer aggregation, because it occurs only in haemoglobins having the distal histidine. It is thus proposed that this amino acid residue might have had a significant role for the development of low-oxygen-affinity haemoglobins in vertebrates.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 209-214 |
| Number of pages | 6 |
| Journal | Journal of Molecular Evolution |
| Volume | 6 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 1975 |
Keywords
- Distal Histidine
- Haem-Haem Interaction
- Oxygen Affinity
- Protomer Aggregation
ASJC Scopus subject areas
- Ecology, Evolution, Behavior and Systematics
- Molecular Biology
- Genetics