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. Author manuscript; available in PMC: 2012 Dec 4.
Published in final edited form as: Biochim Biophys Acta. 2010 Jul 21;1804(11):2136–2145. doi: 10.1016/j.bbapap.2010.07.013

Table 2.

Thermodynamic parameters derived from thermal unfolding studies of catalase–peroxidase from Magnaporthe grisea (MagKatG1) and Synechocystis PCC6803 followed by UV–Vis-(Soret region), circular dichroism (CD, Soret and far-UV region) and differential scanning calorimetry (DSC).

Method ΔG°H2O
(kJ mol−1)
 ΔHm
(kJ mol−1)
 ΔSm
(kJ mol−1 K−1)
 Cp
(kJ mol−1 K−1)
 Tm
(°C)
MagKatG1 SynKatG MagKatG1 SynKatG MagKatG1 SynKatG MagKatG1 SynKatG MagKatG1 SynKatG
UV–Vis 8.3 8.5 231.5 234.6 0.73 0.74 9.2 9.1 41.3 43.0
[θ]412 8.9 8.6 236.2 234.7 0.75 0.74 9.5 9.2 41.4 43.5
[θ]222 8.2 8.5 232.9 234.0 0.73 0.73 9.3 9.4 43.7 44.0
DSC 47.2 56.9 850.9 978.6 2.66 3.04 8.4 8.0 45.0 48.1
N-terminal domain 19.5 25.0 372.6 456.7 1.17 1.43 – – 43.0 44.5
C-terminal domain 27.6 31.8 478.3 521.9 1.49 1.62 – – 45.8 48.1

ΔG°H2O, conformational stability; ΔHm, ΔSm, enthalpic and entropic changes at midpoint transition (T=Tm).