title: Aplysia oxymyoglobin with an unusual stability property: involvement of two kinds of carboxyl groups.
abstract: Unlike mammalian oxymyoglobins, Aplysia MbO2 is extremely susceptible to autoxidation, and its pH dependence is also unusual. Kinetic formulation has revealed that two kinds of dissociable group with pK1 = 4.3 and pK2 = 6.1, respectively, at 25 degrees C are involved in the stability property of Aplysia MbO2. In order to characterize thermodynamically these dissociation processes involved, the effect of temperature on K1 and K2 was studied by analyzing the pH dependence for the autoxidation rate of Aplysia MbO2 in 0.1 M buffer over the pH range of 4-11, and at 15, 25 and 35 degrees C. The resulting thermodynamic parameters for each group were both those to be expected for the ionization of a carboxyl group; the delta H degrees value being numerically much less than 1 kcal.mol-1, or zero in practice, but being associated with a large negative value of delta S degrees of the order of -20 cal.mol-1.K-1. Taking into account the fact that Aplysia myoglobin contains only a single histidine residue corresponding to the heme-binding proximal one, we can unequivocally conclude that the two kinds of the dissociable group involved in the unusual stability of Aplysia MbO2 must both be carboxyl groups, the protonation of these groups being responsible for an increase in its autoxidation rate in the acidic pH range.
authors.affiliation: Biological Institute, Tohoku University, Sendai, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Matsuoka
authors.forename: K
authors.initials: K
authors.lastname: Shikama
mesh_terms: D000818:Animals; D001048:Aplysia; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D009211:Myoglobin; D013816:Thermodynamics
chemical_list: D009211:Myoglobin; C017595:oxymyoglobin