Table 1. Kinetic Parameters Associated with the Set of Aptananozymes I–V and Control Systems, and Dissociation Constants of the Respective Dopamine and Aptananozymesa.
aptananozyme | Vmax (μM min–1) | KM (μM) | kcat (s–1) | Kd (μM) |
---|---|---|---|---|
IV | 2.05 ± 0.11 | 113 ± 13 | 3.8 ± 1.0 | 0.76 ± 0.03 |
III | 1.95 ± 0.22 | 207 ± 67 | 6.5 ± 0.8 | 0.95 ± 0.04 |
II | 1.73 ± 0.26 | 247 ± 36 | 5.7 ± 0.8 | 1.20 ± 0.06 |
I | 1.66 ± 0.13 | 305 ± 67 | 5.5 ± 0.9 | 1.65 ± 0.03 |
V | 0.89 ± 0.31 | 310 ± 56 | 3.0 ± 0.5 | 0.93 ± 0.05 |
scrambled DBA/pA-AuNPs | 0.43 ± 0.05 | 334 ± 89 | 1.4 ± 0.6 | – |
separated DBA/pA-AuNPsb | 0.2 ± 0.06 | – | 0.7 ± 0.08 | – |
All experiments were performed in a 5 mM MES buffer solution, pH 5.5, that included 5 mM MgCl2, 100 mM NaCl, and 5 nM of the respective aptananozymes or control system and 5 mM H2O2. Error bars derived from N = 3 experiments.
The separated pA-AuNPs/DBA system shows pseudo-first-order kinetics: k = 0.7 s–1.