Binding of carbon monoxide to alpha-hemocyanin and beta-hemocyanin from Helix pomatia.
The binding of carbon monoxide to alpha and beta-hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium-ion effect), however, were just as strong as in the case of the binding of oxygen. For alpha-hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the protein.
D000818:Animals; D001665:Binding Sites; D002118:Calcium; D002248:Carbon Monoxide; D006372:Helix, Snails / Q000378:metabolism*; D006433:Hemocyanins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D012908:Snails / Q000378:metabolism*
D002248:Carbon Monoxide; D006433:Hemocyanins; D002118:Calcium