title: Effects of magnesium sulfate on an unfolding step of human cyanomet myoglobin.
abstract: The effects of magnesium sulfate (MgSO4) on an unfolding step of human cyanomet myoglobin (Mb) were examined for wild-type and three L-->A mutant Mbs. The unfolding was induced at acidic pH (3.6-4.5) with various concentrations of MgSO4 (0-2 M). The monophasic process was monitored by visible absorption spectroscopy. We observed quite nonlinear delta G not equal to-[MgSO4] relations for all the Mbs. delta G not equal to-[MgCl2] relations were also determined for a comparative study. Thermodynamic evaluation of the results indicated that an upward reflection of delta G not equal to-[MgSO4] relations in high [MgSO4] is caused by the strong Hofmeister effect of the salt. Results obtained for three mutants (L29A, L72A, and L104A) at pH 4.0 and 4.5 were consistent with our previous observation that the structure of the transition state is determined by the stability of Mb cores in the balance with the pH conditions of unfolding (T. Konno and I. Morishima. 1993. Biochim. Biophys. Acta. 1162:93-98).
authors.affiliation: Division of Molecular Engineering, Graduate School of Engineering, Kyoto University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Konno
authors.forename: I
authors.initials: I
authors.lastname: Morishima
mesh_terms: D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007930:Leucine; D008278:Magnesium Sulfate / Q000494:pharmacology*; D008433:Mathematics; D008786:Metmyoglobin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000187:drug effects; D016297:Mutagenesis, Site-Directed; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000187:drug effects; D013816:Thermodynamics
chemical_list: D011994:Recombinant Proteins; C007177:cyanometmyoglobin; D008786:Metmyoglobin; D008278:Magnesium Sulfate; D007930:Leucine