Table 1. Kinetic parameters of the various supramolecular nucleoapzyme structures with respect to the oxidation of dopamine (1) to aminochrome (2) in the presence of H₂O₂ ^a .

Entry	Code	k cat b (10–3 s–1)	K M (μM)	V max (μM min–1)	k cat/k2 c
1	0	7.3 ± 0.4	1.1 ± 0.2	0.32 ± 0.02	8.1
2	3t	9.4 ± 0.5	1.7 ± 0.3	0.42 ± 0.02	10.4
3	4t	27.0 ± 1.0	6.7 ± 0.7	1.20 ± 0.04	30.0
4	5t	16.5 ± 0.7	3.7 ± 0.5	0.73 ± 0.03	18.3
5	6t	17.0 ± 0.8	5.0 ± 0.7	0.76 ± 0.04	18.9
6	7t	12.8 ± 0.3	3.5 ± 0.3	0.57 ± 0.01	14.2
7	8t	12.3 ± 0.3	7.0 ± 0.5	0.55 ± 0.01	13.6
8	9t	5.2 ± 0.4	4.0 ± 1.0	0.23 ± 0.02	5.8
9	4r	6.1 ± 0.5	c.n.b.d. d	0.27 ± 0.02	6.7
10	5r	5.9 ± 0.7	c.n.b.d. d	0.26 ± 0.03	6.5
11	6r	7.2 ± 0.4	c.n.b.d. d	0.32 ± 0.02	7.9
12	ss9	4.4 ± 0.2	c.n.b.d. d	0.19 ± 0.01	4.9

^aConditions: 0.5–64 μM dopamine, 100 μM H₂O₂; 0.74 μM active catalyst; buffer: 50 mM MES, pH = 5.5, 200 mM KCl, 2 mM MgCl₂.

^b k _cat = V_max/[catalyst] = V_max/0.74.

^cThe rate constant for the hGQ DNAzyme (1) is: k₂ = (0.9 ± 0.1) × 10^–3 s^–1.

^dc.n.b.d. stands for ‘could not be determined’.