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. Author manuscript; available in PMC: 2012 Jun 28.
Published in final edited form as: Biochemistry. 2011 Jun 2;50(25):5790–5798. doi: 10.1021/bi2006306

Table 2.

Thermodynamic Parameters for Binding of ATP and AdoCbl to D180X ATR

ATPa
 AdoCblb
Site 1 Site 2 Sites 1 and 2
KD (μM) 0.48 ± 0.02 4.01 ± 0.61 44.1 ± 3.2
ΔHo (kcal/mol) −0.27 ± 0.02 −3.40 ± 0.04 5.61 ± 0.26
TΔSo (kcal/mol) 7.86 ± 0.91 3.41 ± 0.04 11.10 ± 0.63
ΔGo −8.12 ± 0.90 −6.87 ± 0.61 −5.49 ± 0.89
Nc (sites) 0.38 ± 0.08 1.43 ± 0.07 2.07 ± 0.07
a

ITC data for ATP binding were fitted to a 2-site model.

b

The isotherms for binding of AdoCbl to D180X ATR were best fit to a single-binding-site model.

c

N represents the number of unique sites described by the fitting model.