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Protein Science, Vol 3, Issue 8 1253-1260, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature

D. S. COHEN and G. J. PIELAK
Department of Biochemistry and Biophysics, Campus Box 7260, University of North Carolina, Chapel Hill, North Carolina 27599

Absorbance-detected thermal denaturation studies of the C102T variant of Saccharomyces cerevisiae iso-1-ferricytochrome c were performed between pH 3 and 5. Thermal denaturation in this pH range is reversible, shows no concentration dependence, and is consistent with a 2-state model. Values for free energy ({Delta}G(D)), enthalpy ({Delta}H(D)), and entropy ({Delta}S(D)) of denaturation were determined as functions of pH and temperature. The value of {Delta}G(D) at 300 K, pH 4.6, is 5.1 +/- 0.3 kcal mol(-1). The change in molar heat capacity upon denaturation ({Delta}C(p)), determined by the temperature dependence of {Delta}H(D) as a function of pH (1.37 +/- 0.06 kcal mol(-1) K(-1)), agrees with the value determined by differential scanning calorimetry. pH-dependent changes in the Soret region indicate that a group or groups in the heme environment of the denatured protein, probably 1 or both heme propionates, ionize with a pK near 4. The C102T variant exhibits both enthalpy and entropy convergence with a {Delta}H(D) of 1.30 kcal mol(-1) residue(-1) at 373.6 K and a {Delta}S(D) of 4.24 cal mol(-1) K(-1) residue(-1) at 385.2 K. These values agree with those for other single-domain, globular proteins.
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