TABLE 1.
The binding constant (Kb), number of binding sites (n), the biomolecular quenching rate constant (kq), the Stern-Volmer constant (KSV), ΔS˚, ΔH˚ and ΔG˚ for the interaction BSA with Ho-complex and Dy- complex at 295, 298, 301, and 303 K.
| (K)T | KSV × 10−4 (M−1) | kq × 10−12 (M−1s−1) | n | Kb × 10−5 (M−1) | ∆G˚ (kJ/mol) | ΔH˚ (kJ/mol) | ΔS˚ (J/mol.K) | |
|---|---|---|---|---|---|---|---|---|
| 295 | 8.04 ± 0.04 | 8.04 ± 0.04 | 1.17 | 6.60 ± 0.03 | −32.86 ± 0.06 | |||
| Ho | 298 | 6.82 ± 0.05 | 6.82 ± 0.05 | 1.16 | 5.13 ± 0.04 | −32.57 ± 0.04 | −81.87 ± 0.04 | −185.94 ± 0.06 |
| 301 | 6.35 ± 0.03 | 6.35 ± 0.03 | 1.13 | 3.31 ± 0.05 | −31.80 ± 0.03 | |||
| 303 | 3.95 ± 0.03 | 3.95 ± 0.03 | 1.15 | 2.63 ± 0.03 | −31.44 ± 0.03 | |||
| 295 | 6.94 ± 0.04 | 6.94 ± 0.04 | 1.17 | 6.02 ± 0.06 | −32.64 ± 0.02 | |||
| Dy | 298 | 6.47 ± 0.05 | 6.47 ± 0.05 | 1.15 | 4.17 ± 0.03 | −32.06 ± 0.04 | −111.63 ± 0.06 | −264.41 ± 0.04 |
| 301 | 3.84 ± 0.04 | 3.84 ± 0.04 | 1.15 | 2.69 ± 0.05 | −31.29 ± 0.06 | |||
| 303 | 2.45 ± 0.06 | 2.45 ± 0.06 | 1.16 | 1.77 ± 0.03 | −30.45 ± 0.05 |