The reaction of Octopus vulgaris hemocyanin with exogenous ligands: proposal of an allosteric model for the binding of cyanide and thiourea to the 11 S subunit.
Octopus vulgaris hemocyanin in 11 S aggregation state binds oxygen following a noncooperative oxygen saturation curve with Hill coefficient n = 1. Under the same conditions the equilibrium and kinetics of the reaction with cyanide and other ligands are indicative of an anticooperative behavior displaying different characteristics for the different ligands. The data are consistent with an induced-fit type allosteric model which assumes for the 11 S subunit of O. vulgaris hemocyanin an annular structure made up by five identical domains each containing one binding site whose reactivity is near-neighbor regulated.
D000818:Animals; D001665:Binding Sites; D003486:Cyanides / Q000378:metabolism*; D004735:Energy Transfer; D006433:Hemocyanins / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D049831:Octopodiformes; D010100:Oxygen / Q000032:analysis; D013890:Thiourea / Q000378:metabolism*
D003486:Cyanides; C021724:oxy-beta-hemocyanin; D006433:Hemocyanins; D013890:Thiourea; D010100:Oxygen