Thermodynamics of the reaction of ferric myoglobin from Aplysia limacina with azide and fluoride. Dependence of enthalpy changes on pH.
The effect of pH on the enthalpy changes for binding of azide and fluoride to ferric myoglobin from Aplysia limacina, which lacks the distal histidine, has been investigated. Over the whole pH range explored (3.8 to 9.5), -delta H degrees values for the formation of the hemoprotein-ligand complexes are: (1) much greater than the variations in -delta G degrees; (2) always negative; and (3) show a dependence upon pH characterized by a maximum for azide and a minimum for fluoride binding, centered at pH 4.55 (identical to pHch). This value agrees well with that expected from the linear correlation between pHch and the simple function "Lys+Arg-Glu-Asp-2" proposed by Beetlestone and others. Data reported here greatly extend the pH range for which the linear correlation between the net charge of the macromolecule and pHch has been found to hold, and indicate unequivocally that the pH dependence of -delta H degree for the binding of anionic ligands does not uniquely require the presence of the histidyl residue at the distal position.
D000818:Animals; D001048:Aplysia / Q000378:metabolism*; D001386:Azides / Q000378:metabolism*; D005459:Fluorides / Q000378:metabolism*; D006420:Hemeproteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008786:Metmyoglobin / Q000378:metabolism*; D013816:Thermodynamics
D001386:Azides; D006420:Hemeproteins; D008786:Metmyoglobin; D005459:Fluorides