Cooperative binding
Cooperative binding is when the number of small molecules binding to a macromolecule depends on the concentration of those small molecules around the macromolecule.[1]
This is a type of molecular binding, which is where molecules attach to each other in a stable way without decaying or breaking that bond rapidly.
Example
A popular example of cooperative binding is between haemoglobin and oxygen.[2] In the lungs, there is a very high concentration of oxygen in the alveoli of the lungs. So the oxygen bonds to haemoglobin to form oxyhaemoglobin.[3] When this travels around the body in the blood and reaches areas of low oxygen concentration, the oxygen is released from the haemoglobin.[4]
Cooperative Binding Media
Original figure from Christian Bohr, showing the sigmoidal increase of oxyhemoglobin as a function of the partial pressure of oxygen.
References
- ↑ Heinz Decker & Kensal E van Holde 2011. Oxygen and the evolution of life Heidelberg; New York: Springer, p. 84
- ↑ Michael L Johnson; Jo M Holt; Gary K Ackers 2011. Biothermodynamics, Part D Amsterdam, Netherlands; Boston, MA: Elsevier/Academic Press, p. xiii
- ↑ Pamela C. Champe; Richard A. Harvey; Denise R. Ferrier 2005. Biochemistry Philadelphia: Lippincott Williams & Wilkins, p. 29
- ↑ Pauling L. 1935. The oxygen equilibrium of hemoglobin and its structural interpretation. Proceedings of the National Academy of Sciences of the United States of America 21 (4): 186–191. [1] Archived 2018-06-04 at the Wayback Machine