TABLE 4.
Thermodynamic parameters of APS binding to the AtAPSK·SO42− complex, G111A, and G113A proteins
All titrations were performed at 17 °C as described under “Experimental Procedures.” ITC data were fit to either a one-site binding model (n = number of sites) or a two-site binding model.
Protein | Titrant | K1 | K2 | ΔH1 | ΔH2 |
---|---|---|---|---|---|
μm | kcal mol−1 | ||||
AtAPSK·SO42− | APS | 3.78 ± 2.55 n = 1.98 ± 0.04 | −8.0 ± 0.6 | ||
AtAPSK G111A | APS | 102.7 ± 30.1 | 439.0 ± 131.8 | −6.4 ± 2.2 | −2.7 ± 1.9 |
AtAPSK G113A | APS | 130.0 ± 45.6 | 365.9 ± 93.7 | −9.1 ± 4.6 | −5.4 ± 2.5 |