Table 2.
peroxide substrate |
k1 (ROOH) [M-1 s-1] × 105 |
k2 (TryX) [M-1 s-1] × 106 |
k
cat
[s−1] |
Km (ROOH) [μM] |
Km (TryX ) [μM] |
---|---|---|---|---|---|
TDPX1 | |||||
hydrogen peroxidea |
0.80 ± 0.18 | 6.9 ± 1.5 | 15.4 ± 1.4 | 193 ± 27 | 2.2 ± 0.3 |
hydrogen peroxideb |
1.0 ± 0.06 | 6.2 ± 0.6 | 21.4 ± 7.4 | 211 ± 74 | 3.5 ± 1.2 |
t-butyl hydroperoxidea |
0.068 ± 0.0019 | 5.2 ± 1.6 | 15.2 ± 2.0 | 2244 ± 353 | 2.9 ± 0.5 |
cumene hydroperoxidea |
0.79 ± 0.09 | 6.2 ± 0.7 | 16.2 ± 0.7 | 207 ± 14 | 2.6 ± 0.2 |
TryP1 | |||||
hydrogen peroxideb |
13 ± 2 | 1.7 ± 0.1 | 8.8 ± 1.0 | 6.3 ± 0.8 | 4.9 ± 0.6 |
t-butyl hydroperoxideb |
8.9 ± 0.8 | 1.8 ± 0.1 | 7.8 ± 0.8 | 10.5 ± 1.4 | 4.3 ± 0.5 |
cumene hydroperoxideb |
11 ± 1.5 | 3.0 ± 0.2 | 8.6 ± 0.5 | 8.0 ± 0.7 | 2.8 ± 0.2 |
The initial velocities of 30 individual assays with different TryX and hydroperoxide concentrations were globally fitted to the equation describing a ping-pong mechanism (see “experimental procedures”). Values are the means and standard errors obtained by non-linear regression.
The data were calculated using the integrated Dalziel rate equation (see “experimental procedures”). Values are the weighted means and standard deviations of two independent experiments obtained by linear regression.